Tabela de conteúdos
Biomoléculas
Parâmetros gerais
As biomoléculas são formadas por bioelementos como oxigênio, carbono, nitrogênio, fósforo e outros elementos fundamentais, os quais são resultantes de metabolismos primários e secundários por parte dos organismos vivos.
Os metabolismos primários são aqueles de biomoléculas que fazem parte dos processos vitais e essenciais de um organismo vivo, por sua vez os metabolismos secundários abrangem as moléculas do metabolismo primário, porém, incluem também o desenvolvimento de funções complementares às funções essenciais.
A maioria das biomoléculas são derivadas de hidrocarbonetos e possuem átomos de hidrogênio substituídos por uma grande variedade de grupos funcionais. Esses grupos são responsáveis por conferir propriedades químicas e específicas a molécula. Alguns exemplos dessas biomoléculas são os álcoois, que possuem um ou mais grupos hidroxila; as aminas, com o grupo amina, e entre outros. Há também moléculas que são polifuncionais, isto significa que contêm dois ou mais tipos de grupos funcionais, cada qual com suas características [1].
Afinidade com solvente universal (H2O)
Biomoléculas polares se dissolvem facilmente em água pois podem substituir interações entre moléculas de água (água - água) por outra energeticamente mais favorável (água - soluto). A única exceção são moléculas apolares que além de serem pouco solúveis em água são incapazes de formarem interações do tipo água - soluto. Elas entretanto, formam agregados. (principios das biomoleculas - referencia)
A água é um solvente polar e devido a isso, consegue dissolver a maioria das biomoléculas, que em geral são compostos carregados ou polares. Esses compostos são divididos em 2 grupos, compostos hidrofílicos e compostos hidrofóbicos [1].
Hidrofílicas
As substâncias hidrofílicas são aquelas que apresentam afinidade com a água e assim se dissolvem nesta. O caráter polar da água a torna um solvente universal para materiais polares e iônicos.
As substâncias tem sua capacidade de solubilidade aumentada quando apresentam grupos funcionais que formam ligações de hidrogênio com a molécula de água, como a carbonila (C=O), hidroxila (OH), amônio(NH3+) ou carboxilato (COO-). Alguns exemplos ricos de grupos funcionais como estes, são as proteínas, ácidos nucleicos e carboidratos [2].
Hidrofóbicas

Por sua vez, as substâncias hidrofóbicas têm características apolares e portanto, não se dissolvem quando estão em água. A hidrofobia provoca agregação de substâncias apolares na água e assim algumas macromoléculas, como proteínas e ácidos nucleicos, adotam suas formas em resposta a esse efeito [2].
Classificações
As biomoléculas podem ser classificadas como orgânicas ou inorgânicas
- Biomoléculas orgânicas são aquelas que são sintetizadas por seres vivos e estão presentes apenas nestes, como proteínas, carboidratos, lipídios e ácidos nucleicos.
- Biomoléculas inorgânicas são aquelas que podem estar presentes nos seres vivos ou em qualquer outro elemento inerte, como a água.
Além desta classificação, grande parte das biomoléculas são ditas do grupo das macromoléculas, que têm alto peso molecular e estrutura química complexa, e se formam a partir da união de moléculas menores (ou subunidades) mais simples, que determinam suas características estruturais.
Estas podem ser classificadas em quatro grandes temas, são estes:
- Carboidratos e Polissacarídeos
- Ácidos Graxos e Lipídeos
- Aminoácidos e Proteínas
- Bases Nitrogenadas e Ácidos Nucleicos
Carboidratos e Polissacarídeos
Os carboidratos são as moléculas em maior abundância no Planeta Terra. São os principais elementos da alimentação em várias partes do mundo e sua oxidação é a principal via de produção de energia na maioria das células fotossintéticas [1].
As unidades mais simples de um carboidrato são denominadas monossacarídeos [1]. Os monossacarídeos são formados por uma única unidade poli-hidroxicetona ou poli-hidroxialdeido. Monossacarídeos encordoados de infinitas maneiras formam os denominados polissacarídeos [2]. Os polissacarídeos são polímeros que contêm mais de 20 unidades de monossacarídeo [1].
Outra unidade de um carboidrato, são os oligossacarídeos que são formados por unidades curtas de monossacarídeos, ou resíduos, unidas por ligações características chamadas de ligações glicosídicas[1].
Carboidratos
Carboidratos geralmente são compostos pelos elementos carbono, hidrogênio e oxigênio (fórmula empírica [CH2O]n, com n maior ou igual a 3), e em alguns casos pode conter nitrogênio, fósforo ou enxofre. Essa molécula está presente na formação de todas as células dos organismos, na forma de revestimento, no desenvolvimento das funções específicas das proteínas, na comunicação celular nos eucariontes superiores, na formação da base sanguínea nos humanos e entre outras funções, sendo assim uma ferramenta importante na funcionalidade celular [1][2][3].
Estrutura
Uma das características mais importantes nos carboidratos está relacionado com as inúmeras possibilidades de formação estrutural. Essa característica está associada com a sua composição resultante dos monossacarídeos,que são pequenas moléculas formadas por três a nove carbonos ligados a grupos hidroxila. Quando acontece a ligação entre monossacarídeos (carboidratos simples), isso resulta em diversas formas de estruturas denominadas oligossacarídeos. Tal formação é vantajosa uma vez que resulta em novas estruturas e novas funções, tornando assim os monossacarídeos ricos em informação [1][2][3].
Monossacarídeos
Os monossacarídeos são cetonas ou aldeídos, que consistem em dois ou mais grupos hidroxilas. Os Di-hidroxiacetona (cetose), D-gliceraldeído (aldose) e o L-gliceraldeído (aldose), são formados por três carbonos, sendo designados como triose; logo os de quatro, cinco, seis e sete carbonos, são denominados respectivamente como tetroses, pentoses, hexoses e heptoses. Um dos monossacarídeos mais conhecidos são as hexoses, como a glicose, fonte de energia fundamental para todas as formas de vida; e a frutose, utilizada como derivada da glicose dentro das células [1][2][3].
Aldose
Será definido como aldose o grupo carbonila está localizado na extremidade da cadeia de carbonos (grupo aldeído) [1].
Cetose
Será definido como cetose quando o grupo carbonila está localizado em qualquer outra posição da cadeia de carbonos (grupo cetona) [1].
Em soluções aquosas, todos os monossacarídeos com cinco ou mais átomos de carbono ocorrem como estruturas cíclicas. A formação dessas estruturas acabam formando derivadas chamados hemiacetais ou hemiacetais [1].
Anômeros
Anômeros são formas isoméricas de monossacarídeos que diferem apenas na configuração do carbono hemiacetal ou hemicetal [1].
Oligossacarídeos
Os oligossacarídeos serão constituídos de cadeias curtas de unidades de monossacarídeos, unidas por ligações glicosídicas. Na extremidade redutora, se localiza a unidade de monossacarídeo com seu carbono anomérico que não está envolvido em uma ligação glicosídica [1].
Polissacarídeos
Os polissacarídeos são polímeros de açúcar que apresentam em sua estrutura mais de 20 unidades de monossacarídeos. Alguns polissacarídeos apresentam cadeia linear (açúcares) ou ramificada (glicose), tais exemplos são formados por ligações repetidas de D-glicose, entretanto, se diferem quanto a suas ligações e porventura diferem em suas funções. Os polissacarídeos ou glicanos, diferem entre si nas unidades de monossacarídeos repetidos, no tamanho de sua cadeia, nos tipos de ligação que unem esses monossacarídeos e no grau de ramificação do mesmo.
Os polissacarídeos não possuem massa molecular definida, diferentemente das proteínas, sendo está diferença uma consequência derivada da sua formação. Logo, a síntese do polissacarídeo não possui um “molde” e é baseada nas enzimas catalizadoras. Este processo influencia na variação do comprimento do polissacarídeo. Um exemplo de polissacarídeo é o amido, presente em células vegetais; e o glicogênio, presente em célula animal. Ambos são polissacarídeos de armazenamento e denominados como homopolissacarídeos, devido ao fato de existir apenas uma espécie monométrica com intuito de armazenagem de monossacarídeos para formação de energia. As moléculas de amido e glicogênio são hidratadas, devido a presença de hidroxila que favorece a formação de ligação de hidrogênio com a água [1].
Celulose
A celulose (C6H10O5)n é um polímero estrutural na parede celular das plantas, sendo uma substância fibrosa e insolúvel em água, não ramificada e homopolissacarídeo linear. É composta por fitas planas em anéis de glicose, seguidos um pelo outro, permitindo que o grupo C3-OH dos resíduos de glicose formem ligações de hidrogênio com o 05, originando assim o anel do próximo resíduo. Os resíduos de D-glicose têm configuração beta, diferente das amilose que se encontram com configurações alfa. Possuir a configuração beta significa que os resíduos de glicose na celulose estão ligados por ligações glicosídicas (beta-1,4), resultando em uma estrutura macroscópica e propriedades distintas da amilose. Por formar cadeias compridas e lineares, formando a fibrina, sendo esta resistente a tensão, derivada das interações de Van der Wall e da ligação de hidrogênio, formando uma estrutura altamente coesa, resultando na sua utilização como matéria prima estrutural, principalmente na industria têxtil. Outra característica da celulose qual é derivada da sua ligação (beta-1,4), está relacionada com impossibilidade de digestão pela grande maioria dos animais vertebrados, que ocorre pela falta da enzima(celolase) para hidrolisar a ligação e consequentemente digeri-la, como é o caso dos ruminantes [2] [3].
Quitina
A quitina (C8H13O5N)n é uma homopolissacarídeo linear composto por resíduos de N-acetilglicosamina em ligação,(beta-1,4), e diferem da celulose quimicamente por ter substituição do grupo hidroxila em C-2, pelo grupo amina acetilado. A IUPAC, nomeia de 2-(acetilamino)-2-desoxi-D-glicose. Assim como a celulose a quitina tem sua função empenhada em formar fibras longas e isso resulta em sua característica estrutural, como nos artrópodes, sendo a principal fonte do exoesqueleto desses animais [2] [3].
Lactose
Apresenta nome sistemático O-b-d-galactopiranosil-(1,4)-d-glicopiranose e, por ter um carbono anomérico livre no resíduo de glicose, é considerado um açúcar redutor, ou seja, sacarídeos anoméricos que não formam glicosideos [2].
Sacarose
A sacarose é o dissacarídeo mais abundante, podendo ser encontrado, por exemplo, como a principal forma pela qual os carboidratos são transportados nas plantas. Apresenta nome sistemático O-a-d-glicopiranosil-(1,2)-b-d-fructosuranosídeo, sendo considerado um açúcar não redutor, pois o carbono anomérico de cada açúcar participa da ligação glicosídeos [2].
Amido
Como já abordado, o amido é um polissacarídeo, e contém dois tipos de polímeros de glicose, chamados de amilose e amilopectina. O primeiro consiste em cadeia longa, com massa molecular elevada e não ramificada, já o segundo consiste em uma alta ramificação de sua cadeia e massa molecular também elevada [3].
Glicogênio
O glicogênio é um polímero de subunidade de glicose, sendo este mais ramificado e mais compactado que o amido. Sua presença no corpo humano se dá no fígado, nas células hapatócitos, tendo sua presença na forma de grânulos, cuja função está associada com a ligação do mesmo em enzimas; sendo tais enzimas responsáveis pela síntese ou pela degradação do próprio glicogênio. Ao ser usado como fonte de energia o glicogênio remove a glicose da extremidade não redutora, tal extremidade não possui grupo CL-OH, e essa ação permite que as enzimas de degradação atuem nas extremidades acelerando a conversão do polímero em monossacarídeo [2] [3].
Glicoconjugados
Uma outra importante característica dos polissacarídeos e dos oligossacarídeos é sua capacidade de transportar informação, seja pela comunicação entre a célula e sua matriz ou pela sinalização direcionada à proteína no que diz respeito ao transporte dentro da célula. Praticamente toda célula eucariótica (que possui um núcleo organizado e estrutura mais complexa) apresenta uma ligação entre cadeias de oligossacarídeos e componentes da membrana plasmática, formando uma camada de carboidratos que atua como uma superfície cheia de informações que são expelidas para o meio exterior pela célula, chamada de glicocálice. Esse processo informativo engloba situações como a resposta de imunidade de um corpo, a cicatrização de ferimentos, a coagulação sanguínea, dentre outros processos celulares. Na grande maioria desses casos, o carboidrato responsável por carregar a informação está ligado covalentemente a uma proteína ou a lipídeo, dando origem ao chamado glicoconjugado.
Esses glicoconjugados podem ser divididos em três tipos: os proteoglicanos, as glicoproteínas e os glicoesfingolipídeos. Os proteoglicanos são macromoléculas presentes na superfície da célula ou na matriz da parte exterior, cujas estruturas unidas covalentemente a uma proteína de membrana ou a uma proteína secretada, que são os principais componentes de todas as matrizes extracelulares. As glicoproteínas, por sua vez, apresentam oligossacarídeos de complexidades variadas, e são unidos a uma proteína por ligações covalentes. Elas são comumente encontradas na parte externa da membrana plasmática, na matriz extracelular e, também, no sangue. Por fim, os glicoesfingolipídeos são os componentes da membrana cujos grupos hidrofílicos (isto é, que apresentam alta capacidade de absorção de líquidos) da cabeça são oligossacarídeos. O cérebro e os neurônios são exemplos ricos em glicoesfingolipídeos, que auxiliam na condução nervosa. Os três tipos de glicoconjugados serão discutidos mais aprofundadamente a seguir [1].
Proteoglicanos
São moléculas que exercem um processo de organizar os tecidos e, também, influenciar diversas atividades celulares, como por exemplo a adesão e a ativação de fatores relacionados ao crescimento. Muitas delas são secretadas para a matriz extracelular (MEC), entretanto, também existem algumas que desempenham papéis integrais de membrana.
Durante sua liberação para o meio extracelular, os proteoglicanos desenvolvem um mecanismo que permite que a célula seja capaz de alterar rapidamente as características em sua própria superfície. Tal mecanismo consiste em uma relação estritamente ligada entre uma protease da matriz extracelular e uma fosfolipase que, graças à ação dessas enzimas, torna possível uma regulação nas células em proliferação, tais como células cancerosas. O processo da liberação dos proteoglicanos faz parte do reconhecimento e da adesão intracelular, bem como na proliferação e na diferenciação das células.
Ainda, algumas dessas moléculas têm a propriedade de se organizar e formar agregados proteoglicanos, que constituem-se basicamente de supermoléculas de proteínas centrais, agrupadas e ligadas a uma única molécula de ácido hialurônico. Tal organização abrange as proteínas fibrosas da matriz, como colágeno, elastina e fibronectina, formando toda uma rede de ligações que garantem à MEC atributos como força e elasticidade [1].
Glicoproteínas
Constituem-se basicamente de conjugados carboidrato-proteína, onde a maior quantidade da molécula é composta por glicosaminoglicanos dos proteoglicanos e a menor parte composta por glicanos. Nelas, o carboidrato pode constituir de 1 até 70% da composição da massa de glicoproteína. Além disso, praticamente metade de todas as proteínas dos mamíferos é glicolisada, sendo que 1% de todos os genes pertencentes aos mamíferos é capaz de codificar as enzimas envolvidas no processo de síntese e ligação dessas cadeias de oligossacarídeos.
As glicoproteínas estão abundantemente presentes na superfície externa da membrana plasmática, sendo chamadas de glicoproteínas de membrana. As mucinas são exemplos dessas moléculas, que podem conter numerosas cadeias de oligossacarídeos ligadas a oxigênios e estão comumente presentes na maioria das secreções, sendo responsáveis, por exemplo, pela propriedade escorregadia do muco. Elas, também, fazem parte da maioria das proteínas contidas no sangue, como as imunoglobulinas, responsáveis pela geração de anticorpos, e até mesmo dos hormônios estimulantes da tireoide [1].
Glicoesfingolipídeos
Assim como as proteínas, alguns lipídeos também apresentam cadeias de oligossacarídeos, covalentemente ligados ou não. Devido essa similaridade com as glicoproteínas, as porções oligossacarídicas dos lipídeos de membrana também são comumente encontrados na superfície externa da membrana plasmática.
Nas células bacterianas gram-negativas, há a presença de lipopolissacarídeos em sua membrana externa. Tais moléculas são os principais alvos do sistema de imunidade dos vertebrados, que produzem anticorpos que agirão diretamente nelas em resposta a uma infecção bacteriana. Devido a isso, pode-se considerar essas moléculas como importantes agentes na determinação de linhagens bacterianas [1].
Ácidos Graxos e Lipídeos
Lipídeos
Os lipídeos formam o quarto grupo principal de moléculas que são encontradas em todas as células. Os lipídios possuem grande variedade estrutural, maior que as outras classes de moléculas biológicas [2].
Os lipídios contem características químicas/física que a fazem ser hidrofóbicas(baixa solubilidade em água) e levemente solúvel em solventes orgânicos que quando hidrolisados fornecem ácidos graxos entre outros compostos[2].
Esse grupo possui diversas funções biológicas, as gorduras(glicerídeos de ácidos saturados, que em temperatura ambiente, são sólidas e produzidas por animais) e os óleos ( glicerídeos de ácido insaturado, que em temperatura ambiente, são líquidas e produzidas por plantas) são responsáveis por serem as principais fontes de armazenamento de energia em muitos organismos, com finalidade de reserva energética, controle de temperatura, funções macro e micro celulares entre outras muitas funções.
Os fosfolipídeos e esteróis são os elementos principais das estruturas das membranas biológicas. Ainda há outras funções que são desempenhadas por lipídeos que se apresentam em pequena quantidade, como transportadores de elétrons, cofatores enzimáticos e âncoras hidrofóbicas para proteínas [1].
Grande parte dos lipídeos se caracterizam como compostos anfipáticos (ou anfifílicos), isto significa que a molécula que os constitui apresenta uma porção polar, hidrofílica, e uma porção apolar, hidrofóbica.
Ácidos graxos
Os ácidos graxos são ácidos carboxílicos com grupos laterais de longas cadeias de hidrocarbonetos [2]. O grupo carboxila presente em sua estrutura compõe a sua região polar, enquanto a cadeia carbônica compõe sua região apolar.

Os ácidos graxos mais comuns nas plantas e em animais superiores, onde apresentam em sua cadeia carbônica 16 (C16) ou 18 (C18) carbonos, sendo comum que estas cadeias carbônicas sejam formadas por um número par de carbonos, devido à forma com a qual esses compostos são sintetizados. Além disso, é pouco habitual apresentarem cadeias carbônicas menores que 14 carbonos e superiores a 20 carbonos.
As propriedades físicas dos ácidos graxos e dos lipídeos deles derivados dependem da ocorrência ou não de insaturações (presença de ligações duplas) na cadeia de hidrocarboneto e do seu comprimento [4]. Nos ácidos graxos monoinsaturados a ligação dupla costuma ocorrer entre C-9 e C-10 (Δ9), enquanto nos ácidos graxos poli-insaturados as outras ligações duplas costumam ser Δ12 e Δ15, não sendo esta uma regra. Os ácidos graxos insaturados naturais têm, em sua grande parte, duplas ligações com a configuração geométrica cis (átomos de hidrogênio do mesmo lado da dupla ligação), atribuindo à cadeia uma dobra rígida, a qual faz com que os agregados formados sejam menos compactos e, consequentemente, menos estáveis.
Os ácidos graxos saturados são moléculas altamente flexíveis que podem adotar uma ampla variedade de conformações, pois há uma rotação relativamente livre ao redor de cada ligação C-C [2].
De forma geral, a temperatura de fusão dos ácidos graxos diminui com o número de insaturações e aumenta de acordo com o comprimento da cadeia, e consequente aumento da massa molecular. Além disso, o tamanho da cadeia carbônica influi diretamente no grau de insolubilidade do composto, uma vez que esta confere o caráter apolar a molécula.
Classificação
Triacilgliceróis
Triacilglicerol (TAG) são constituídas de três moléculas de ácidos graxos ligadas a uma molécula de glicerol. Os triacilgliceróis são denominados e diferem-se de acordo com a identidade e a posição dos seus três resíduos de ácido graxo [2].
As moléculas de triacilglicerol representa como a gordura é armazenada no organismo. Em humanos, a maior parte está armazenada no tecido adiposo e representa cerca de 21 a 26% da massa corpórea [2].O TAG também está presente em pequenas quantidades no plasma e no músculo esquelético [5][6].

Além disso, os triacilgliceróis são apolares e, portanto, são armazenados em uma forma quase anidra, enquanto os carboidratos muito mais polares são mais hidratados. Com efeito, 1 g de glicogênio seco liga-se a cerca de 2 g de água. Em consequência, um grama de reservas de gorduras quase anidras armazena 6,75 vezes mais energia do que um grama de glicogênio hidratado, provavelmente o motivo pelo qual os triacilgliceróis, e não o glicogênio, foram selecionados na evolução como principal reservatório de energia [3].
Os adipócitos são responsáveis pela síntese e armazenamento de gordura no organismo e são constituídos quase que totalmente por moléculas de gordura, permitindo que animais sobrevivam até 3 meses sem se alimentar [2].

A camada gordurosa subcutânea também fornece isolamento térmico e energia em animais que hibernam, em alguns animais recém nascidos e em muitos mamíferos adultos, sobretudo aqueles adaptados a climas frios. A energia do gradiente de prótons, normalmente capturada como ATP, é liberada na forma de calor à medida que os prótons fluem através de UCP-1 para a matriz mitocondrial. Essa via dissipativa de prótons é ativada quando a temperatura corporal central começa a cair. Em resposta à queda da temperatura, a liberação de hormônios resulta na liberação de ácidos graxos a partir dos triacilgliceróis que por sua vez ativam a termogenina [3].
Glicerofosfolipídeos
Os principais tipos de lipídeos de membranas são os fosfolipídeos e os glicolipídeos.

Fosfolipídeos
Os lipídeos são o principal componente lipídico das membranas biológicas [2]. Os fosfolipídeo são constituídos por quatro componentes: um ou mais ácido graxo, uma plataforma à qual se fixam os ácidos graxos, um álcool ligado ao fosfato e um fosfato [3]. Como já citado, ácidos graxos são hidrofóbicos, porém o restante da molécula possui característica hidrofílica, permitindo a interação com água.
Os fosfoglicerídeos possuem diversas funções nas células, como estabelecer barreira de permeabilidade, influenciar os processos catalíticos e a comunicação entre o meio intra e extracelular pela transdução celular e a interação lipídeo com a proteína [7].
Os glicerofosfolipídeos são determinados pelos produtos de reações de hidrólise catalisadas por fosfolipases.Os lisofosfolipídeos são detergentes potentes que rompem membranas celulares, dessa forma lisando as células [2].
Glicolipídeos
Os glicolipídeos são lipídeos que se diferenciam pois uma ou mais açúcares estão ligadas ao grupo hidroxila primária. Os glicolipídeos mais complexos contêm uma cadeia ramificada de até sete resíduos de açúcar. Os glicolipídeos são orientados de modo totalmente assimétrico, com os resíduos de açúcar sempre no lado extracelular da membrana [3].
Os glicolipídeos influenciam as propriedades das proteínas ligadas à membrana e servem como precursores importantes de mensageiros diacilglicerol e inositol trifosfato [8].
Esfingolipídeos
Esfingolipídeos também são componentes das membranas e assemelham-se com a estrutura dos glicerofosfolipídeos. No entanto, não contêm glicerol e em sua maioria o esqueleto básico é derivado do aminoálcool (C18), uma longa cadeia de hidrocarboneto também chamada de esfingosina, onde as ligações duplas têm a configuração trans [2][4].

A ceramida é um composto que atua como precursora dos esfingolipídeos e é originada a partir da ligação amídica do grupo amino da esfingosina com um ácido graxo. Deste modo, três tipos de lipídeos são formados a partir da ligação de uma estrutura polar ao carbono 1 da ceramida, as esfingomielinas, cerebrosídeos e gangliosídeos [2][4].

As esfingomielinas são ceramidas em que o grupo polar pode ser fosfocolinas ou fosfoetanolaminas, onde são classificadas junto aos glicerofosfolipídeos como fosfolipídeos. Constituem entre 10 a 20 mol% dos lipídeos da membrana plasmática [1][2]. Ressalta-se que “a bainha de mielina que reveste e isola eletricamente muitos axônios das células nervosas é particularmente rica em esfingomielinas” [2].
Enquanto que os cerebrosídeos possuem apenas um único açúcar ligado à ceramida, que pode ser glicose ou galactose. Os que tem glicose são caracteristicamente encontrados nas membranas plasmáticas das células em tecidos não neurais, os que têm galactose são encontrados nas membranas plasmáticas das células em tecido neural. Dessa forma, são classificados como glicoesfingolipídeos, dividindo-se em galactocerebrosídeos e glicocerebrosídeos [1][2].
Já os últimos lipídeos formados por tais ceramidas são os gangliosídeos, o mais complexo entre os esfingolipídeos. Eles possuem como grupo cabeça polar os oligossacarídeos e um ou mais resíduos do ácido N-acetilneuramínico (Neu5Ac), que por sua vez é comumente chamado de ácido siálico [1]. Estes lipídeos “são os componentes principais das membranas da superfície celular e constituem uma fração significativa (6%) dos lipídeos cerebrais” [2].
Contudo, os gangliosídeos agem como receptores específicos para determinados hormônios glicoproteicos hipofisários que regulam diversas funções fisiológicas importantes. Além disso, atuam como receptores de algumas toxinas proteicas bacterianas, indicando que eles têm importante significado médico e fisiológico. Ainda é importante ressaltar que existem evidências de que os gangliosídeos possuem função importante no crescimento, na diferenciação dos tecidos e na carcinogênese, ou seja, desempenham reconhecimento célula-célula. Enquanto que sua degradação pode causar doenças hereditárias de armazenamento de esfingolipídeos [2].
Por fim, os esfingolipídeos que receberam tal nome em homenagem ao monumento da Esfinge por parecer tão enigmático quanto, são identificados em pelo menos 60 tipos diferentes nas membranas celulares de humanos, sendo proeminentes na membrana plasmática dos neurônios e em sítios de reconhecimento na superfície celular [1]. Além disso, algumas porções de carboidrato de certos esfingolipídeos definem os grupos sanguíneos humanos, ou seja, definem o tipo de sangue do indivíduo. Enquanto os gangliosídeos “apresentam pontos de reconhecimento para moléculas extracelulares ou superfícies de células vizinhas” [1].
Esteróides
Os esteróides são lipídeos estruturais presentes nas membranas e sua maioria é de origem eucariótica. Apresentam um núcleo tetracíclico característico, derivado do ciclopentanoperidrofenantreno, que consiste em quatro anéis não planares fusionados [1][2][4].

Dentre os esteróides, o colesterol é o principal nos tecidos animais, é anfipático, com um grupo cabeça polar (grupo hidroxila em C-3) e um “corpo” hidrocarboneto apolar (núcleo esteróide e a cadeia lateral hidrocarbonada no C-17) [1]. Além do colesterol ser o mais abundante nos tecidos animais, constituindo de 30 a 40 mol% dos lipídeos, ele atua como precursor à síntese de todos os outros esteróides, incluindo hormônios esteroídicos, sais biliares e vitamina D. De todo modo, ele ainda possui função estrutural e é determinante das características de fluidez das membranas celulares [2][4].

No corpo humano, em função dos hormônios esteróides serem insolúveis em água, eles são transportados pelas lipoproteínas plasmáticas, ligadas predominantemente à ácidos graxos, formando os ésteres de colesterol, que por sua vez, também é sua forma de armazenamento dentro das células [4]. Destaca-se que em outros eucariotos como plantas e fungos encontram-se esteróis semelhantes, estigmasterol e ergosterol, respectivamente. Enquanto os procariotos contém pouco esterol ou nem mesmo possui tal lipídeo [1] [2].
O colesterol possui inúmeras funções, como: formação da bile e precursor de hormônios esteróides, substâncias que regulam grande variedade de funções fisiológicas [9], que por sua vez são classificados como glicocorticoides, aldosterona, mineralocorticoides, androgênios e estrogênios.
Os glicocorticoides afetam o metabolismo de carboidratos, proteínas e lipídeos, além de influenciar em algumas funções vitais como por exemplo reações inflamatórias e a capacidade de lidar com o estresse. Enquanto que a aldosterona e alguns outros mineralocorticoides regulam a excreção de sal e água pelos rins e, por último, os androgênios e estrogênios que afetam o desenvolvimento e a função sexual [2]. Para tal, os glicocorticoides e os mineralocorticoides são sintetizados pelo córtex (camada externa) da glândula suprarrenal, enquanto o androgênios e estrogênios são sintetizados pelos testículos e ovários, respectivamente e em menor grau pelo córtex suprarrenal [2].
Bicamadas lipídicas
Raramente os lipídeos são encontrados como moléculas livres nos seres vivos, sendo comum a sua associação com outras moléculas, principalmente outros lipídeos [2]. Dessa forma, os lipídeos se agregam formando micelas ou bicamadas lipídicas.
Quando moléculas anfipáticas são postas em soluções aquosas, seus grupos de hidrocarbonetos (hidrofóbicos) evitem o contato com a água, enquanto sua suas cabeças (hidrofílicas) sofrem solvatação. Dessa forma, agregados globulares são formados, sendo estes denominados de micelas.
A forma e tamanho dessas micelas estão intimamente ligados com as características das moléculas anfipáticas que os formam. Assim como a forma e tamanho, o número de moléculas que constituem a micela depende das moléculas que os formam, no entanto, para muitas substâncias esse número fica na casa de várias centenas, uma vez que poucas moléculas iriam expor as caudas hidrofóbicas à água e muitas moléculas formariam um centro oco, desfavorável energeticamente [2].
Alternativamente, as preferências fortemente opostas dos componentes hidrofílicos e hidrofóbicos dos lipídeos de membranas podem ser satisfeitos com a formação de uma bicamada lipídica, composta de duas lâminas de lipídeos [3]. As caudas hidrofóbicas de cada lâmina individual interagem umas com as outras, formando um interior hidrofóbico que atua como barreira de permeabilidade [3].

As moléculas lipídicas de uma bicamada podem mover-se ao longo da bicamada, em processos chamados de difusão transversal e difusão lateral. Na difusão transversal, também denominada de movimento de ponta-cabeça, a cabeça polar do lipídeo passa por toda a cauda apolar, passando de uma lâmina para outra. Esse fenômeno é raro de ocorrer e, quando ocorre, é caracterizado por uma velocidade muito lenta.

Em contrapartida, na difusão lateral os lipídeos se movem ao longo do plano da bicamada com elevada rapidez. Nesse caso, ocorre a troca de uma molécula lipídica por sua vizinha, na mesma lâmina da bicamada, sendo esse um fenômeno mais simples e comum de ocorrer devido a mobilidade dos lipídeos nesse sentido, conferindo à bicamada lipídica o título de fluido bidimensional.
O aspecto de fluidez de uma bicamada lipídica está diretamente ligado à temperatura. A chamada temperatura de transição é quem irá ditar a fluidez da bicamada. Esta temperatura é determinada em função do tamanho da cadeia de lipídeos e do grau de saturação de seus componentes. De forma geral, bicamadas lipídicas com temperatura abaixo da temperatura de transição tornam-se uma espécie de gel sólido e perdem sua fluidez, enquanto bicamadas lipídicas acima da temperatura de transição tem suas moléculas com alta mobilidade e fluidez [2].

Em uma membrana biológica típica, as bicamadas são formadas por diferentes lipídios, cujas caudas são diferentes tamanhos ou flexionadas devido a presença de insaturações[2], dando um aspecto desorganizado ao elemento.
Aminoácidos e Proteínas
As proteínas são responsáveis por controlar praticamente todos os processos que ocorrem em uma célula. Proteínas são macromoléculas biológicas mais abundantes que ocorrem em todas as células e em todas as partes das células. As proteínas são o meio pelo qual às informações genéticas são expressas [1].
“ A estrutura primária de uma proteína é sua sequência de aminoácidos” [2]. As proteínas de cada organismo, desde os mais simples aos mais complexos são construídas a partir de um conjunto onipresente de 20 aminoácidos. Um ponto marcante das proteínas é que as células são capazes de produzir proteínas com propriedades e atividades diferentes ligando os 20 aminoácidos, com combinações e sequências completamente diferentes [1].
Discutindo sobre a estruturas das proteínas, surgem outros três níveis de complexidade. São eles:
-Estrutura secundária;
-Estrutura terciária;
-Estrutura quaternária [2].
Aminoácidos
Os aminoácidos são as unidades básicas das proteínas de cada organismo, desde bactérias até seres humanos. Os 20 aminoácidos onipresentes nas proteínas são os α-aminoácidos. Além dos 20 comuns, há outros aminoácidos, sendo que alguns não constituem uma proteína e outros são resíduos modificados de uma proteína. [1] Muitos aminoácidos incomuns são gerados a partir da sintetização da cadeia polipeptídica. [2]
Em 1806 foi descoberto o primeiro aminoácido, a asparagina, e em 1936 foi descoberto o último dos 20 aminoácidos comuns, a treonina. Como são moléculas antigas e ubiquas, foram captados pela evolução para uma variedade de propósitos nos sistemas vivos. [2] [3]
Estrutura
Um α-aminoácido, aminoácido comum ou aminoácido padrão, consiste em um átomo de carbono, chamado de carbono α, ligado a um grupo amino, a um grupo carboxila, um átomo de hidrogênio e a um grupo R diferenciado, que é chamado, normalmente, de cadeia lateral. [3] Porém, existem duas exceções, a glicina, que possui outro átomo de hidrogênio no lugar do grupo R e a prolina, que apresenta um grupo amino secundário, mas por questão de uniformidade, essas exceções são chamadas de α-aminoácidos. [2]

Os quatro grupos (amino, carboxila, átomo de hidrogênio e o grupo R) se ligam em volta do átomo de carbono α, portanto os α-aminoácidos são quirais, podendo se organizar de maneira a formar dois arranjos espaciais, chamados de isômeros L e isômeros D, sendo que apenas os aminoácidos L formam as proteínas. A diferença de um aminoácido comum para outro está nas estruturas de suas cadeia laterias, ou seja, no grupo R de cada aminoácido.
Classificação
A forma mais útil de classificar os 20 aminoácidos comuns é de acordo com as propriedades do grupo R. Há quatro tipos principais de aminoácidos: (1) aminoácidos hidrofóbicos com grupo R apolar, (2) aminoácidos polares com grupo R neutro, (3) aminoácidos carregados positivamente e (4) aminoácidos carregados negativamente: [3]
- Aminoácidos hidrofóbicos com grupo R apolares: dentre estes aminoácidos, o mais simples é a glicina, que como cadeia lateral, apresenta apenas um átomo de hidroênio, assim, por ter dois átomos de hidrogênio ligados ao carbono α, esse aminoácido é o único aquiral. O segundo aminoácido mais simples desta classificação é a alanina, que possui o grupo metila como cadeia lateral. Outros tipos de aminoácidos que pertencem a esta classificação são a valina, leucina, metionina, fenilalanina entre outros. [3]
- Aminoácidos polares com grupo R neutro: são seis aminoácidos polares que não possuem carga no grupo R. Há os aminoácidos que possuem grupo hidroxila ligados em uma cadeia lateral hidrofóbica, são eles: a serina, a treonina e a tirosina. Estes três, por apresentarem grupo hidroxila, são reativos com alguns aminoácidos hidrofóbicos, sendo a serina reativa com a alanina, a treonina com a valina e a tirosina reativa com a fenilalanina. Nesta classificação, estão aminoácidos que, no lugar do ácido carboxílico, apresentam uma carboxamida terminal, são eles a asparagina e a glutamina. E o último aminoácido pertencente a esta classificação é a cisteína, que possui estrutura próxima com a da serina, porém, não possui grupo hidroxila, apresentando um grupo sulfidríla, sendo este grupo mais reativo.[3]
- Aminoácidos carregados positivamente: são aminoácidos que apresentam cargas positivas completas, logo, são altamente hidrofílico (são atraídos pelas moléculas de água). Pertence a esta classificação a lisina, que apresenta uma amina primária em uma das extremidades, também está presente neste grupo o áminoácido arginina, que possui um grupo guanidínio. [3]
- Aminoácido carregados negativamente: são dois aminoácidos que pertencem a esta classificação, o aspartato e o glutamato, que apresentam cadeias laterais ácidas. Estes dois aminoácidos possuem carga negativa, pois, em pH fisiológico, não apresentam um próton em sua cadeia lateral. Porém, existem proteínas que possuem a importante capacidade de aceitar prótons nestas cadeias laterais. [3]
Simbologia e Nomenclatura
A designação dos aminoácidos pode ser feita através de um símbolo, que é a primeira letra do seu nome, ou símbolos convencionados, pode ser feita, também, pela abreviação das primeiras três letras de seus nomes, com algumas exceções, como o triptofano que é designado por Trp. [3]
Tabela dos 20 aminoácidos comuns:
NOME | SÍMBOLO | ABREVIAÇÃO | NOMENCLATURA |
---|---|---|---|
Glicina ou Glicocola | Gly, Gli | G | Ácido 2-aminoacético ou Ácido 2-amino-etanóico |
Alanina | Ala | A | Ácido 2-aminopropiônico ou Ácido 2-amino-propanóico |
Leucina | Leu | L | Ácido 2-aminoisocapróico ou Ácido 2-amino-4-metil-pentanóico |
Valina | Val | V | Ácido 2-aminovalérico ou Ácido 2-amino-3-metil-butanóico |
Isoleucina | Ile | I | Ácido 2-amino-3-metil-n-valérico ou ácido 2-amino-3-metil-pentanóico |
Prolina | Pro | P | Ácido pirrolidino-2-carboxílíco |
Fenilalanina | Phe ou Fen | F | Ácido 2-amino-3-fenil-propiônico ou Ácido 2-amino-3-fenil-propanóico |
Serina | Ser | S | Ácido 2-amino-3-hidroxi-propiônico ou Ácido 2-amino-3-hidroxi-propanóico |
Treonina | Thr, Tre | T | Ácido 2-amino-3-hidroxi-n-butírico |
Cisteína | Cys, Cis | C | Ácido 2-bis-(2-amino-propiônico)-3-dissulfeto ou Ácido 3-tiol-2-amino-propanóico |
Tirosina | Tyr, Tir | Y | Ácido 2-amino-3-(p-hidroxifenil)propiônico ou paraidroxifenilalanina |
Asparagina | Asn. | N | Ácido 2-aminossuccionâmico |
Glutamina | Gln | Q | Ácido 2-aminoglutarâmico |
Aspartato ou Ácido aspártico | Asp | D | Ácido 2-aminossuccínico ou Ácido 2-amino-butanodióico |
Glutamato ou Ácido glutâmico | Glu | E | Ácido 2-aminoglutárico |
Arginina | Arg | R | Ácido 2-amino-4-guanidina-n-valérico |
Lisina | Lys,Lis | K | Ácido 2,6-diaminocapróico ou Ácido 2, 6-diaminoexanóico |
Histidina | His | H | Ácido 2-amino-3-imidazolpropiônico |
Triptofano | Trp, Tri | W | Ácido 2-amino-3-indolpropiônico |
Metionina | Met | M | Ácido 2-amino-3-metiltio-n-butírico |
Ionização dos aminoácidos
Existem dois grupos de aminoácidos ionizáveis, que, dependendo do pH do meio em que se encontram, podem ser protonados ou desprotonados. Em meio com pH muito ácido, ambos os grupos estão protonados e em meio com pH muito básico, os dois grupos estão desprotonados. As cargas elétricas de cada grupo ionizável de um aminoácido dependem, além do pH do meio, do valor do pKa e quando somadas representam a carga total do aminoácido. [1]
Um aminoácido, que contém um grupo R ionizável que atua em conjunto com os grupos amino e carboxila funciona como um ácido e base fraco. Agora, quando há a dissolução em água com pH neutro, de um aminoácido que não contém o grupo R ionizável, o aminoácido atua como um íon bipolar, podendo agir como ácido ou base, substâncias com essa característica são chamadas, normalmente, de anfólitos. [4]
Aminoácidos incomuns
Proteínas podem conter, além dos 20 aminoácidos comuns, resíduos que são modificações de resíduos comuns já incorporados, esses são os aminoácidos incomuns, como a 4-hidroxiprolina, que é derivada da prolina e pode ser encontrada em paredes celulares de células vegetais. Derivado de quatro diferentes resíduos Lys, a desmosina é o aminoácido incomum mais complexo e pode ser encontrada na proteína elastina. Alguns resíduos desses aminoácidos em uma proteína podem ser modificados transitoriamente para alterar as funções da proteína. A adição de grupos fosforil, metil, acetil, adenilil e ADP-ribosil a resíduos de aminoácidos específicos aumentam ou diminuem a atividade de uma proteína.
Cadeia polipeptídica
Para formar cadeias, os aminoácidos são ligados em sequência, através de um processo onde uma molécula de água é eliminada, fazendo com que ocorra uma ligação amida (CO¬NH), que é conhecida como ligação peptídica, formando uma cadeia polipeptídica, onde cada aminoácido é chamado de resíduo. A ligação peptídica é plana e em uma ligação de dois aminoácidos ocorre o alinhamento no mesmo plano de seis átomos, são eles: o carbono α e o grupo CO do primeiro com o grupo NH e o carbono α do segundo aminoácido.
Uma ligação peptídica plana pode ter configuração cis ou configuração trans. Na trans os dois átomos de carbono α estão em lados opostos, já na configuração cis, os átomos de carbono α estão no mesmo lado da ligação peptídica.

Já a ligação entre o grupo amino e o carbono α, são ligações simples, assim como a ligação entre o grupo carbonila e o carbono α. Estas ligações simples podem ser rotacionadas permitindo que a estrutura de cada cadeia polipeptídica seja ajustada, a rotação da ligação entre o nitrogênio e o carbono gera um ângulo de torção Phi (φ), enquanto a rotação da ligação entre o carbono α e o carbono do grupo carbonila gera um ângulo psi (ψ). O trajeto da cadeia é determinada por estes dois ângulos (φ, ψ), que são considerados positivos se a rotação ocorrer no sentido horário. Porém, como pode acontecer colisões estéricas entre os átomos nem todas as rotações e combinações de φ e ψ são possíveis.

Como, em uma cadeia polipeptídica, um grupo α amino está em uma extremidade e um grupo α carboxila está na outra extremidade, as cadeias apresentam polaridade. Em uma cadeia polipeptídica há uma cadeia principal, que apresentam alto potencial para pontes de hidrogênio e há uma parte que corresponde as cadeias laterais, chamada de parte variável. Muitas cadeias polipeptídicas apresentam de 50 à 2.000 resíduos de aminoácidos, as cadeias com massa molecular abaixo de 10.000 são chamadas de polipeptídeos e as com massa molecular mais elevada são chamadas de proteínas.
Proteínas

Proteínas são macromoléculas essenciais em todos os processos biológicos, além de serem as mais versáteis e possuírem funções cruciais para os organismos. Dentre essas funções estão algumas como catalisadores, transportadores, fornecimento de suporte mecânico, proteção imunológica e armazenadores de outras moléculas, como por exemplo, a hemoglobina que armazena oxigênio. Elas também exercem funções reguladoras intracelulares e extracelulares ajudando a manter as condições e transportando informações.
Para decifrar o funcionamento de cada proteína, a compreensão de sua estrutura é fundamental, assim como as principais macromoléculas, as proteínas são compostas pelo conjunto de estruturas menores, no caso das proteínas, denominadas aminoácidos. Apesar da análise da composição das proteínas ser fundamental, por possuírem 20 aminoácidos dos quais as proteínas são feitas, ao contrário dos ácidos nucleicos, não apresentam estruturas regulares e uniformes. Os aminoácidos ligam-se através de ligações covalentes, denominadas ligações peptídicas, formando cadeias polipeptídicas. Nestas ligações ocorrem reações de condensação, ou seja, o grupo carboxila presente no aminoácido da cadeia polipeptídica reage com o grupo amina do aminoácido a ser ligado, liberando assim água (H2O).
A sequência dos aminoácidos pode ser analisada diretamente ou via sequenciamento do DNA, como será discutido abaixo. Em ambos os métodos, a informação sobre o sequenciamento permite o entendimento sobre as propriedades físicas e químicas das proteínas.
Diversidade polipeptídica

Uma proteína difere de outra por diversos fatores, sendo que a estrutura de uma proteína é uma das principais diferenças. Os níveis de organização de uma proteína podem descrever as proteínas, através de suas estruturas primárias, secundária, terciária e quaternária, sendo a secundária a estrutura tridimensional que é formada por pontes de hidrogênio entre os aminoácidos mais próximos, já a ligação entre aminoácidos mais distantes na sequência, fornece a estrutura terciária. [2] [1]
Estrutura primária: A estrutura primária é o nível mais simples da estrutura da proteína, é simplesmente uma sequência de aminoácidos em uma cadeia polipeptídica, sendo a única que pode ser determinada pelas reações químicas, porém, por conta da complexidade em se analisar tais reações, até hoje, poucas proteínas conseguiram ser identificadas por tal método. Como a sequência dos aminoácidos é determinante para a identificação da proteína, a hidrólise total das proteínas evidencia os aminoácidos presentes em tal macromolécula, porém, nada diz sobre o sequenciamento. [2]
Um exemplo que une a ideia da individualidade das proteínas por conta dos diversos aminoácidos existentes e suas possíveis combinações é o caso da alteração de um único aminoácido associado à anemia falciforme, doença hereditária que afeta as hemácias. Nesse exemplo, o ácido glutamato, que é o sétimo aminoácido da hemoglobina β é substituído por uma valina. Sendo assim, apenas a modificação de um aminoácido faz com que a função da protéina seja modificada.
Estrutura secundária: É tridimensional e se refere a arranjos das cadeias polipeptídicas que se enovelam, dessa forma formam diferentes conformações podendo ser torcidas, dobradas ou enroladas entre si. As primeiras estruturas regulares que foram propostas, em 1951, foi a α-hélice e a folha β.
Na estrutura α-hélice as cadeias polipeptídicas formam um arranjo helicoidal visto que ligações de hidrogênio intramoleculares ocorrem a cada volta de modo a unir aminoácidos opostos e conferindo a forma de hélice, dessa forma a parte central é altamente aglutinada, no lado externo da hélice estão presentes os grupos R livre para interagirem.

A estrutura folha β é formada pelo alinhamento entre cadeias polipeptídicas que são novamente unidas por ligações de hidrogênio que se formam entre os grupos carbonila e amino. A direção na qual as cadeias se encontram altera a ordem de ligação, dessa forma é possível subdividir a estrutura folha β em paralela e antiparalela.

Em seguida foram identificadas outras estruturas, como a volta β e a laço Ω, que mesmo não sendo periódicas como as primeiras, contribuem para a estrutura final da proteína. Estas estruturas regulares são formadas por ligações de hidrogênio entre aminoácidos próximos na sequência linear. Existe a possibilidade de estruturas secundárias se combinam, formando as estruturas supersecundárias, que estão presentes em muitas proteínas.[2] [3]
Estrutura terciária: A estrutura terciária se refere ao trajeto geral de uma cadeia de uma proteína e pode indicar as funções biológicas e as origens das proteínas. Se origina do enovelamento das estruturas secundárias, que, em muitas proteínas é feito de maneira assimétrico e com núcleo constituído de resíduos apolares, enquanto a parte externa da estrutura terciária é composto por resíduos polares e apolares, isso revela que o enovelamento de uma cadeia polipeptídica ocorrem de maneira que as cadeia polares e carregadas ficam na superfície e as cadeias laterais dá cadeia vão para o interior da estrutura, devido aos resíduos que são hidrofóbicos e tendem à serem excluídos em um meio aquoso. [2] [3]
O resultado da estrutura terciária é corresponde principalmente por interações entre os grupos R dos aminoácidos que compõem a proteína. Torna-se necessário caracterizar as ligações que ocorrem, sendo basicamente todas as ligações não covalentes. Os grupos R que apresentam mesma carga se repelem enquanto que ao apresentarem cargas opostas, a formação de uma ligação iônica. Há também uma ligação covalente especial nesta estrutura, denominadas de ligações dissulfeto que consiste ligações covalentes entre as cadeias laterais de cisteínas contendo enxofre. Essas ligações funcionam como elos segurança com o intuito de manter determinadas partes de polipeptídeo presas uma as outras. [2]
Estrutura quaternária: O quarto nível de uma estrutura proteica é muito comum de ser encontrado em proteínas que possuem mais de uma cadeia polipeptídica, onde cada uma é denominada de subunidade, que se associam com uma geometria específica e esse arranjo espacial é conhecido como quarto nível da proteína. Geralmente essa ligação entre as subunidades são ligações não covalentes. [2] [3]

Para a classificação dessas proteínas com o nível mais alto de estrutura, temos dois grandes grupo [1]:
- Proteínas fibrosas - são formadas por cadeias polipeptídicas disposta em longos filamentos ou folha. Essas são caracterizadas por serem insolúveis em água devido a alta quantidade de aminoácidos hidrofóbicos, proporcionam resistência e/ou flexibilidade nas estruturas. Geralmente são formadas por um único tipo de estruturas secundária e uma estrutura terciária simples.
- Proteínas Globulares - possuem cadeias polipeptídicas dobradas uma sobre as outras, assim possuem formato globular ou esférico. Elas são compostas geralmente por diversos tipos de estruturas secundárias e possuem função de enzimas, reguladoras e de defesa
Tabela de Proteínas e suas respectivas formações:
PROTEÍNA | NÚMERO DE AMINOÂCIDOS | NUMERO DE CADEIAS POLIPEPTÍDICAS |
---|---|---|
Insulina(bovina) | 51 | 2 |
Lisozima (clara de ovo) | 129 | 1 |
Mioglobina (equina) | 153 | 1 |
Hemoglobina (humana) | 574 | 4 |
Aspartato transcarbamoilase (E. coli) | 2700 | 12 |
RNA Polimerase (E. coli) | 4100 | 5 |
Apolipoproteína B (humana) | 4536 | 1 |
Sequenciamento
O sequenciamento, atualmente, é um processo prático utilizado para determinar a sequência de aminoácidos que compõem uma proteína ou peptídeo. Uma vez que esta ordem é conhecida pode-se compará-la com outras sequências semelhantes, gerando informações importantes para o conhecimento científico.[10] As mutações podem causar a troca de um ou mais aminoácidos da sequência, alterando as funções e características de uma proteína, incluindo patologias. Portanto conhecer e analisar o sequenciamento de uma proteína é importante para explorar as estruturas tridimensionais, que determinam suas funções biológicas e, assim, entender seus mecanismos de ação e auxiliar no desenvolvimento de tratamentos e no diagnósticos de doenças. [2]
Frederick Sanger, em 1953, observou que as proteínas possuem estrutura covalente, após determinar a sequência da insulina bovina, que foi a primeira proteína com sequência conhecida. O sequenciamento foi determinado em uma pesquisa que usou 100g de proteína e durou 10 anos, apresentando como um de seus resultados, que uma sequência é composta apenas de aminoácidos L. Em seguida outras estruturas primárias de proteínas foram sequenciadas, atualmente são conhecidas sequências de, aproximadamente, sete milhões de polipeptídeos e o sequenciamento pode ser feito em poucas horas, utilizando pouca quantidade da proteína. [2] [3]
Para determinar a sequência de aminoácidos de uma proteína é preciso conhecer a sequência unidimensional de bases do DNA, para, em seguida, devido ao enovelamento espontâneo das proteínas, expandir a sequência para o tridimensional. [3]
Evolução
Assim como as demais moléculas, as proteínas passam pelo processo de evolução, sendo aceitas quatro principais formas evolutivas: a seleção natural, as mutações, o fluxo gênico e a deriva genética. Dentre estas, a seleção natural é a que mais causa alterações na busca de homogeneização com o meio ambiente na qual o ser está inserido, e esse processo acontece de forma gradual, junto ao caracteres herdáveis que ajudam na adaptação.
Em estudos mais recentes buscando entender o por quê de algumas proteínas específicas estarem melhor condicionadas a evoluir comparadas à outras, foi observado a partir de grandes bancos de dados; tais como o GenBank, GEO, ENA, PDB e DDJB; que é possível traçar os perfis das proteínas e que as mesmas possuem instabilidade estrutural, regiões de baixas complexidade e grande eficiência traducional. Tais características induziram à conclusão de que uma proteína de fato evolui, e com isso ao invés de considerar equivocadamente o nível de RNAm como o único fator para esse processo, passaram a incluir os fatores genômicos supracitados como também relevantes à mutação genética.
A forma natural de evolução das moléculas proteicas é então dada a partir de processos intrínsecos ao funcionamento da estrutura que as contêm, por alterações nos ácidos nucleicos e, consequentemente, nos aminoácidos que as compõem. Quando as mutações forem significativas a ponto de a resultante ser substancialmente diferente de seu ancestral, a evolução natural está completa para aquela proteína em específico e o processo cíclico se iniciará novamente a partir da mesma, gerando uma cadeia evolutiva e a estruturação de uma árvore filogenética, justamente a expressão do traçado de perfis acima comentado.[11]
As árvores filogenéticas são estruturas gráficas que representam, por ramificações a partir de um ancestral comum, as relações evolutivas de uma cadeia de organismos. Ela é construída a partir de informações a níveis molecular, morfológico e até comportamentais das espécies em estudo, as quais são organizadas de modo a reunir características em comum que foram se reproduzindo em sucessores. Molecularmente, a codificação genética pode ser base para comparação entre compostos e a construção de sua árvore. Abaixo está representada a árvore filogenética do citocromo C, como exemplo desta formação.[12]

Proteínas que partiram de um mesmo ancestral comum, possuem estruturas primárias semelhantes entre si, e conhecer a sequência de uma delas revela as relações evolutivas que a mesma vivenciou ao longo do tempo.
Depois de Margaret Dayhoff, na década de 60, começar a caracterização da evolução das proteínas, muitos algoritmos computacionais foram desenvolvidos para detectar padrões e semelhanças entre as sequências de proteínas que foram evoluindo. Com isso, foi detectado que de 40 a 200 segmentos de resíduos são conservados entre as proteínas durante os processos evolutivos, e essa base formada é denominada domínio da molécula. Se os domínios de duas ou mais proteínas são no mínimo 40% idênticos, elas apresentam relação filogenética e desempenham a mesma função no organismo.[2]
Apesar da ocorrência da mutação genética de maneira natural, há muito tempo a mutação induzida é estudada. Os processos de indução de mutação em proteínas podem ter variadas finalidades, dentre as quais o uso dos agentes produzidos na fabricação de novos medicamentos, pesquisas em produção de biocombustíveis e catalisadores. Mais especificamente sobre o último, um projeto conduzido em 1993 por Frances H. Arnold, engenheira química, teve como objetivo o controle de mutações e processos genéticos para produção de catalisadores, enzimas que aceleram reações químicas no organismo vivo. Toda essa engenharia de proteínas foi realizada a partir da evolução dirigida, ou seja, uma forma de evolução genética não natural. [13]
Em 1985 iniciou-se o período de pesquisa desenvolvida por dois bioquímicos, George P. Smith e Gregory P. Winter, os quais deram continuidade às pesquisas em evolução dirigida, refinando as mutações induzidas a partir de um método denominado phage display, desenvolvido por Smith, focando na produção de proteínas com funções específicas e capacidade de interação com outras proteínas distintas. Essa abordagem abriu espaço para a criação de anticorpos que serviriam para tratamentos terapêuticos de doenças até então consideradas de difícil terapia, como a artrite reumatoide.
Os projetos destes três cientistas apresentam enorme relevância e foram premiados com um Prêmio Nobel de Química, em 2018, conforme publicado pela Revista Fapesp.
A evolução dirigida é então uma das possíveis formas de moléculas progredirem e assumirem novas propriedades, as quais otimizam processos microbiológicos. É um método de ampla aplicação, no qual o código genético das moléculas estudadas passam por ciclos de mutação genética e seleção dos resultados, induzindo os mesmos a cumprir objetivos específicos.
Bases Nitrogenadas e Ácidos Nucleicos
Os nucleotídeos podem ser considerados como “os blocos de construção dos ácidos nucleicos”. Tratam-se de moléculas presentes nas células e apresentam três componentes característicos: uma base nitrogenada (possui extrema importância para diferenciar o RNA do DNA), uma pentose e um ou mais fosfatos. [14]. Vale observar que uma molécula que não apresenta o grupo fosfatado é denominada nucleosídeo, e não nucleotídeo [1]. Para formar o ácido desoxirribonucleico (DNA) se trata da pentose desoxirribose e para formar o ácido ribonucleico (RNA) trata-se da ribose. [15]
“Os nucleotídeos estão envolvidos em todas as facetas da vida celular. Eles estão presentes em reações de oxidação-redução, transferência de energia, sinalização intracelular e reações biossintéticas” [2]. Os principais nucleotídeos são: adenosina trifosfato (ATP) conhecida por ser uma molécula capaz de armazenar energia de praticamente todos os seres, e a adenosina monofosfato (AMP cíclico) conhecida como um segundo mensageiro por servir de ponte para hormônios [16]

Além destas variedades de funções, os nucleotídeos são constituintes dos ácidos nucleicos. Os ácidos nucleicos são dois, o ácido desoxirribonucleico (DNA) e o ácido ribonucleico (RNA) [1]. Os ácidos nucleicos são responsáveis pelo armazenamento e decodificação genética, e também desempenham funções estruturais e catalíticas nas células [2].

Evolucionistas acreditam que o surgimento dos nucleotídeos permitiu a evolução de microrganismos capazes de incorporar e armazenar energia do ambiente e principalmente produzir cópias de si mesmo [2]. A capacidade de armazenar informações genéticas e transmiti-las de uma geração para outra é uma condição fundamental para a vida [2].
Bases nitrogenadas:
São derivadas de dois compostos relacionados, a pirimidina e a purina. A diferença entre a purina e a pirimidina está no número de pontes de hidrogênio que apresentam, sendo 3 pontes presentes nas bases púricas e 2 bases presentes nas bases pirimídicas. Tanto o DNA quanto RNA possuem duas bases púricas principais: adenina (A) e guanina (G), e duas pirimídicas. Para ambos, uma das bases pirimídicas é a citosina (C). No entanto, para o RNA a segunda bases é a uracila (U) e para o DNA a segunda bases é a timina (T) [1].


Pentose:

Trata-se de um açúcar simples (monossacarídeos - glícidos simples) cuja cadeia principal é formada por cinco átomos de carbono. Os ácidos nucleicos possuem dois tipos de pentose, empregadas como convenção. Os ácidos desoxirribonucleicos (DNA) contém 2’-desóxi-D-ribose e os ácidos ribonucleicos (RNA) contém D-ribose. Nos nucleotídeos, as pentoses estão na forma 𝛽-furanose (anel fechado com cinco átomos). O anel pentose não é planar, mas ocorre em uma série de conformações, descritas como “pregueadas”. Em solução, as formas de cadeia reta e em anel da ribose livre estão em equilíbrio. Sabe-se, também, que os anéis de ribofuranose podem existir em quatro conformações pregueada: C-2’ ou C-3’ está no mesmo lado (endo) ou no lado oposto (exo) do plano em relação ao átomo de C-5’ [1].
Grupos Fosfatados:

Os nucleotídeos do DNA e do RNA possuem uma ligação covalente por “pontes” de grupos fosfatados, em uma reação catalisada na célula por DNA polimerase (na replicação do DNA) e por RNA polimerase (na síntese de RNA). A reação ocorre com a OH do C-5’ do grupo fosfato com a OH do C-3’ da pentose do nucleotídeo. O resultado é uma reação covalente denominada ligação fosfodiéster, que liga nucleotídeos consecutivos nos ácidos nucleicos. As ligações possuem a mesma orientação ao longo da cadeia, o que confere uma polarização específica e distinta nas extremidades 5’ (uma hidroxila livre ligada ao fosfato C-5’ da pentose) e 3’ (com uma OH de carbono 3’ da pentose). Como há essa polarização, o esqueleto covalente dos ácidos nucleicos é hidrofílico. Portanto, por convenção, estabelecem que a extremidade 5’ apresenta o primeiro nucleotídeo e a extremidade 3’ apresenta o último nucleotídeo[1].
Ácidos Nucleicos:
Os ácidos nucleicos são cadeias de nucleotídeos e possuem a função de controle celular, pois neles há toda a informação genética[2]. A estrutura primária do DNA consiste basicamente em sua sequência de desoxirribonucleotídeos, enquanto que a estrutura primária do RNA consiste em sua sequência de ribonucleotídeos. A exemplo de um ribonucleotídeo, é necessário apontar a diferença para um desoxirribonucleotídeo. Nesse segundo caso, o grupo -OH no carbono 2’ é substituído por H. A estrutura primária do DNA contém 5 unidades de desoxirribonucleotídeos formados por um carboidrato de cinco carbonos, uma base nitrogenada e um ou mais grupos fosfatos. No DNA temos a presença de uma desoxirribose, uma pentose diferenciada da ribose por ter uma hidroxila a menos que este último açúcar. A principal diferença do DNA para o RNA, além das diferentes pentoses, está nas bases nitrogenadas. A uracila é encontrada apenas no RNA e é ausente no DNA[19].
DNA e RNA
O DNA é uma dupla hélice que armazena informações genéticas do seres. Inicialmente por não haver provas suficientes sobre a relação com armazenamento de material genético, a substância que continha fosfato era chamada de “nucleína”.
O que em meados de 1940 foi mudado, já que com estudos foi possível descobrir a existência de quatro bases nucleotídicas do DNA, que eram encontradas em quantidades diferentes, mas com uma certa relação numérica das bases.
Neste estudo foram indicados algumas conclusões:
- O DNA tem a composição de diferentes bases dependendo de uma espécie para a outra.
- Amostra de diferentes regiões de tecidos da mesma espécie tem a mesma composição de bases e que não mudam com o tempo.
- Toda amostra relativa a DNA celular têm o mesmo número de resíduos de adenosina que é igual ao número de resíduos de timidina, e o número de resíduos de guanosina é igual ao número de resíduos de citidina. Com isso conclui-se que a soma de resíduos de purina é igual à soma dos resíduos de pirimidina. Logo A + T = C + G.
A relação sobre a quantidade de bases serem proporcionais foi muito importante para a construção do modelo tridimensional do DNA, e com isso levantar respostas de como as informações genéticas estão dispostas na substância.
Para isso foi usado um método de difração por raio-x para analisar as fibras do DNA, produzindo um padrão de difração que deu início a dedução de que as moléculas de DNA são helicoidais com duas periodicidades ao longo de seu eixo mais longo a primária de 3,4 Å e a secundária de 34 Å.
A forma de duas hélices conduzem a replicação do DNA de forma mais fácil. Para isso, quando uma célula se divide, cada hélice do DNA serve para moldar a nova síntese da próxima fita complementar.
Síntese que também pode ser responsável pela produção de proteínas, envolvendo outra substância que é o RNA. Substância a qual também possui uma estrutura formada por moléculas de bases nitrogenadas, uma ribose e um fosfato.
O RNA tem como característica de sua estrutura quatro tipos bases nitrogenadas, as purinas, Adenina (A) e Guanina (G) e as pirimidinas, Citosina (C) e Uracila (U).
O mecanismo de replicação, embora pareça simples, é extremamente complexo na célula, necessitando de uma variedade de fatores celulares para ser executado com fidelidade e eficiência.
A conexão entre o DNA e a síntese de quase todas as proteínas é o RNA, pois ele é a transcrição do DNA que possui a sequência complementar. Essa transferência de informação genética é resumida no chamado dogma central da biologia molecular. E assim como o DNA, as fitas de RNA são sintetizadas a partir de ribonucleosídeos trifosfato livres, os quais pareiam com as bases complementares em uma fita do DNA.
O RNA se divide em três tipos, a molécula que codifica o gene é chamado de RNA mensageiro (mRNA) que se transporta para o Ribossomo, onde encontra o RNA ribossômico (rRNA), e já no ribossomo, os nucleotídeos do mRNA se agrupam em três e pareiam com três nucleotídeos de uma nova molécula que é o RNA transportador (tRNA).
DNA e RNA - Diferenças e semelhanças
Tanto o ácido desoxirribonucleico (DNA) quanto o ácido ribonucléico (RNA) são proteínas capazes de armazenar informações genéticas, porém, suas estruturas e funções são diferentes. O DNA é formado por uma dupla fita enroladas em formato de hélice constituída por “um açúcar, um grupo fosfato e uma base nitrogenada — adenina (A), citosina (C), guanina (G) ou timina (T)”. [20]. Além disso, o DNA possui, em suma, a função de transportar informações genéticas, enquanto o RNA é formado por apenas uma fita simples, mas que também é formada por um açúcar, um grupo fosfato e uma base nitrogenada adenina (A), guanina (G), citosina (C) e a uracila (U) e possui a função de permitir que toda a informação armazenada no DNA possa ser transmitida. [14]. Porém, diferentemente do DNA, o RNA possui, no lugar da uracila, timina (T). Além disso, os açúcares presentes em cada uma das proteínas são diferentes, o DNA é formado por desoxirribose e o RNA por ribose. [14]. Enfim, apesar do DNA e RNA serem, ambos, proteínas que podem guardar informações genéticas, cada uma possui características e funções próprias.
Princípio Transformante
Em 1928, o médico inglês Frederick Griffith realizou estudos com a bactéria patogénica Steptococcus pneumoniae (Pneumococos), bactéria causadora de pneumonia nos humanos que é geralmente letal nos ratos. As estirpes dessa bactéria que produzem cápsula de polissacarídeos, geram colónias com aparência lisa (smooth), portanto foram denominadas estirpe S, já as que não produzem foram denominadas estirpe R (rough), devido a aparência rugosa de suas colónias.
Na primeira etapa do experimento, o médico identificou que as estirpes S eram virulentas, pois quando eram inoculadas no ratinho estas provocavam sua morte, já as estirpes R não eram virulentas e, desta forma não matavam os ratos quando inoculadas. Numa etapa seguinte do experimento, as estirpes S foram submetidas ao calor e posteriormente aplicadas nos ratos, assim observou-se que os ratos não morreram, e conclui-se que tais bactérias eram sensíveis ao calor e por consequência morreram. [21]

Griffith isolou as bactérias mortas pela ação do calor da estirpe S e misturou com bactérias vivas da estirpe R, quando esta mistura foi inoculada nos ratinhos observaram o desenvolvimento de pneumonia e a consequente morte dos indivíduos.
O médico prosseguiu e analisou o sangue dos ratos mortos pela mistura de bactérias e, conseguiu isolar bactérias vivas da estirpe S, concluindo que as bactérias da estirpe S conseguiam transmitir sua característica virulenta para as bactérias da estirpe R (não virulenta). Desta forma o contato entre as bactérias não virulentas e as virulentas, mesmo que a segunda estivesse morta, poderia promover uma transformação das bactérias da estirpe R e, esta transmissão de informação ficou conhecida como princípio transformante.
Experimento de Hershey-Chase
Este experimento, que comprova o DNA como princípio tranformante, foi realizado por Alfred Hershey e Martha Chase em 1952 utilizando o bacteriófago T2 que infecta a E. coli. Este bacteriófago foi cultivado em dois meios diferentes: um meio de fósforo pesado-radioativo; o outro meio de enxofre pesado-radioativo. No primeiro meio os DNAs das partículas virais estavam marcados radioativamente pelo fósforo radioativo, já no segundo o que era marcado radiotivamente era o capsídeo, devido à sua natureza proteica, pelo enxofre. Então cada meio foi adicionado à um meio diferente de E. coli e depois do tempo necessário para que os fagos infectassem as células bacterianas os frascos foram agitados e centrifugados para a separação do capsídeo viral e das células bacterianas. Na parte do experimento com os fagos submetidos ao fósforo a radiotividade foi encontrada somente na parte da célula bacteriana, enquanto no experimento com o enxofre aconteceu o contrário onde somente o capsídeo viral vazio estava radioativo. Com isso o experimento provou que, realmente, que o material genético é o DNA. [22]

DNA - Curiosidade
O teste de paternidade utilizando o DNA é o teste mais preciso na atualidade para comprovação ou não de paternidade. Tendo cerca de 99,99% de eficácia para os casos onde o resultado é negativo e de 99,99% a 99,9999% de precisão para quando o suposto pai é realmente o pai biológico. [23] Normalmente não se tem muitos problemas para a realização deste teste, ele pode ser feito com um trio que seria o suposto pai, a mãe e o filho. Nesse caso são retirados,normalmente, o sangue dos três e há uma comparação do DNA do filho com o da mãe e com o pai, esse acaba sendo um teste de maternidade e paternidade ao mesmo tempo, ele pode ser usado quando há uma suposta troca de bebês em maternidade ou quando o filho fica desaparecido e volta depois de algum tempo. [15] Tem o caso onde é feito com o suposto pai e o filho (DUO), nesse caso seria só o teste de paternidade. Esse teste costuma ser mais rápido e mais barato que o teste onde tem o DNA da mãe. O teste de paternidade pode ser feito até mesmo no útero. Mas se forem gêmeos idênticos como supostos pais o teste de DNA não irá ajudar nesse caso. [15] O teste em si consiste na coleta do material genético dos indivíduos envolvidos, após isso é feito uma comparação entre esse material genético para ver se coincidem ou não, caso coincidirem é confirmada a paternidade.
Química dos ácidos nucleicos
Desnaturação
O DNA pode ser sujeito a desnaturação ao ser submetido a altos valores de pH e temperaturas acima de 80º, havendo diminuição da viscosidade. A viscosidade ideal do DNA deve apresentar ph 7 e temperatura ambiente.
O processo de desnaturação ocorre quando há a ruptura das pontes de hidrogênio e, a partir dessa quebra, acontece o desenvolvimento da dupla-hélice que formará duas cadeias simples. Essas cadeias podem ser separadas completamente ou parcialmente (desnaturação parcial). Durante a desnaturação, as ligações covalentes do DNA não são desfeitas, resultando nas duas fitas de DNA separadas.

A renaturação das cadeias pode acontecer de forma natural, quando a temperatura e o pH voltam ao ideal, e os segmentos enrolados das duas cadeias se desenrolam - também pode ser chamado de pareamento. Quando duas cadeias estão totalmente separadas a renaturação acontece em duas etapas. Na primeira etapa, mais lenta, as duas cadeias se encontram formando um segmento de dupla-hélice complementar. Na segunda etapa, mais rápida, há a formação das pontes de hidrogênio, formando a dupla-hélice.
A interação entre bases emparelhadas nos ácidos nucleicos tem como consequência a diminuição na absorção em luz UV e, comparando com nucleotídeos livres, essa absorção se torna ainda menos quando há duas cadeias de ácidos nucleicos pareadas. Esse efeito é chamado de hipocromático. A desnaturação causa o oposto, o efeito hipercromático, que acontece pela alta absorção de luz e expõe as bases nitrogenadas ao meio. Nesse caso, a absorção da luz UV a 260 nm é máxima [1].
A temperatura de desnaturação, ou ponto de fusão, depende de cada espécie de DNA. O pareamento de bases G e C, com três ligações de hidrogênio, demanda maior calor para se dissociar do que o pareamento de bases A e T, com duas ligações de hidrogênio. Ou seja, as duas pontes de hidrogênio das bases A e T são mais fáceis de serem rompidas, pois quanto maior o número de pares C e G com três ligações de hidrogênio, mais alto será seu o ponto de fusão [1].
Formação de híbridos
Híbridos também podem ser formados por ácidos nucleicos diferentes, isso porque o DNA tem a capacidade de se parear com outra cadeia de DNA identificando sequências de DNA semelhantes em duas espécies distintas ou no genoma de uma mesma espécie. A taxa de pareamento é delimitada pela temperatura, pelo comprimento e pela concentração de fragmentos de DNA, concentração de sais e sequência de bases [1]. Essa hibridação retrata o princípio básico para a genética molecular.
Mutações
As purinas e pirimidinas sofrem alterações naturais na sua estrutura covalente, essas mudanças na estrutura do DNA são denominadas mutações. Muitas bases nucleotídicas perdem seus grupamentos exocíclicos, chamado de desanimação (remoção de um grupo amino de uma base).
Bases metiladas
Bases com nucleotídicas do DNA são metiladas, ou seja, são modificadas quimicamente pela ligação de um grupo metil a base citosina. A metilação ocorre mais nas bases adenina e citosina do que na guanina e timina.
Sequenciamento de longas hélices de DNA
Em 1977, Alan Maxam, Walter Gilbert e Frederick Sanger desenvolveram técnicas de sequenciamento de grandes moléculas de DNA através da redução do DNA para quatro grupos de fragmentos. Assim, os comprimentos dos fragmentos correspondem a posições de uma dada base na sequência de DNA.
Ver Também
Ligações Externas
Wikipedia - Biomolécula - Visitado em 03/08/2020.
Discussão
Bom dia pessoal. Pensei em dividir o nosso grupo em subgrupos para cada um trabalhar em temas mais específicos. O que acham?
bom dia Matheus… eu concordo com você!
Acho valido Matheus
Bom dia, Matheus! Concordo com a divisão de subgrupos.
Bom dia Matheus, acho essa ideia ótima!
555
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Bom dia Matheus! Gostei da ideia, como faremos a divisão?
Acho que podemos fazer o solteiro on-line, quer que eu faço?
Pode fazer. Pensei em duas pessoas darem uma introdução à Biomoléculas. E três pessoas para cada um dos subtemas.
Gostei Matheus
ok, ficou assim então.
Marcos,Matheus Mendes e Maria –> Carboidratos e Polissacarídeos
Isabella, Gabriele, e Mariane –> Bases Nitrogenadas e Ácidos Nucleicos
Matheus Cardoso, Lohaynes e Gabriel Ferrari –> Ácidos Graxos e Lipídeos
Guilherme, Felipe e Pedro –> Aminoácidos e Proteínas
Gabriel Bilato e Diogo –> Biomoléculas
Bom dia matheus. Concordo com você, acho que facilita a comunicação
Bom dia Matheus.
Bom dia.
Muito bem! Prossigam com os esforços e qualquer dúvida recorram ao classroom ou a nossos plantões de quarta-feira, pois não recebo notificações da wiki.
Boa tarde pessoal.
O grupo dos lipídeos realizou hoje o upload dos textos referentes ao seu tema. Ainda estamos com algumas dificuldades em realizar o upload de imagens e otimizar o uso das referências na plataforma.
Comentem o que acharam do texto, se existem correções a serem feitas, ou tópicos a serem acrescentados. Estamos à disposição.
As funções que utilizamos são: sobrescrito, subscrito, uso de referências e uso de diferentes tamanhos de título. Quaisquer dúvidas em relação a estes elementos, podem nos procurar.
Att,
Matheus Cardoso, Gabriel Ferrari, Lohaynes Teixeira.
Reunião do grupo 7 realizada hoje (02/07) para divisão de tarefas: Proteínas e diversidade polipeptídica (Welligton, Nicolas, Milton e Matheus) Sequenciamento (Marcus, Felipe e Leandro) Evolução (Nathan, Nathalia, Lucas) Revisão de texto e referências (Ronan, Fernanda, Camila e Francisco)
Divisão para a segunda revisão:
Dupla 1: Revisão de Parâmetros gerais Revisão de Carboidratos e Polissacarídeos Fernando filho Dupla 2: Revisão de Ácidos Graxos e Lipídeos Revisão de Classificação Raphael Dupla 3: Revisão de Aminoácidos Revisão de Proteínas Carol Alves e Carol Previde Dupla 4: Revisão de Bases Nitrogenadas e Ácidos Nucleicos JOICE E MABEL Dupla 5: Revisão de DNA e RNA Thami e abner Dupla 6: Inclusão - DNA e RNA (princípio transformante e experimento de Hershey-Chase) Allan e Daniel
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