Download - Boquímica avançada
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quimotripsina
glicina
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Quimotripsina-cataliza hidrólise de ligaçõespeptídicas
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“lisina”(lys) (L)
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Os átomos envolvidos na ligação peptídica se-encontram no mesmo plano: =180o (trans) ou 0o (cis)
Os ângulos (phi) e (psi) tem “livre” rotação
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Colisões estéricasnão-favoráveis
Algumas combinações dos ângulos (phi) e (psi) não são permitidas.
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DIAGRAM DE RAMACHANDRAN
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Alfa-Hélice
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Alfa-hélice-groupos Rsituados por fora da hélice
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Folha Beta (beta sheet)
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Folha Beta (beta sheet)
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Notar ligação de hidrogênio entre os grupos peptídicos do 1o e 4o
Resíduo. É comum encontrar Pro e Gly nestas estruturas.
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Valores de phi e psi para todos os aminoácidos (menos gly) parapiruvato quinase de coelho.
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Probabilidades relativas para encontrar um tipo de aminoácido numa determinada estrutura secundária
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Estrutura de queratina de cabelo.
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calor
Quero um permanente tipo Vera Loyola!
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Colágeno: um triplo-hélice de cadeias com 3 aminoácidos por volta,helicoidal com sentido de mão esquerda, e super-helicoidal com sentido de mão direita. Composição: 35% gly, 11% ala, 21% pro ou hidroxi-pro.Com repetições gly-X-pro ou gly-X-hidroxi-pro
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Colágeno: componente de tecido conectivo (tendão, cartilagem,matriz orgânica de osso)
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Estrutura de fibroina de seda: estrutura folha beta antiparalela rica em ala e gly.
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Formação de seda nas “espineretes” da aranha.
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Dimensões de albumina sérica humana (585 aminoácidos, 64500 kDa)
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Estrutura de mioglobina de baleia, uma proteína globular típica
Fita (azul = H) modelo “space-filling”
Topografiade superfície
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O grupo heme(anel de protoporfirinaE um ion de Fe2+/3+)
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Determinação de estruturas de proteínas de alta resolução:Cristalografia por raios-X
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Determinação de estruturas de proteínas de alta resolução:R.M.N. = resonância magnética nuclear.
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Proteínas tem flexibilidade conformacional
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Domínios estruturais na proteína troponina C do músculo esquelético
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Dessoxihemoglobina
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Dessoxihemoglobina
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Estrutura Quartenária de Próteínas
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Capsídeo de poliovirus (simetria icosahedral), 30 nm diametro
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Tobacco mosaic virus (300 nm x 18 nm), simetria helicoidal
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Desnaturação de proteínas
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EnovelamentoEspontâneode Proteínas
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Chaperona molecular (GroEL)
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O grupo heme mioglobina
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O grupo heme
Modelo “space-filling”
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Coordenação octahedral do Fe2+ em mioglobina (Mb) e hemoglobina (Hb)
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Coordenação octahedral do Fe2+ em mioglobina (Mb) e hemoglobina (Hb)
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mioglobina
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histidina proximal
histidina distal
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Estado T da hemoglobina
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Pares iônicas que estabilizam o estado T da hemoglobina
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Pares iônicas que estabilizam o estado T da hemoglobina
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dessoxiHb + BPG = estado T
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dessoxiHb = estado T
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oxiHb = HbO2 = estado R
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Eritrócitos normais
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Eritrócitos humanos de forma foice (e outras) encontrados emAnemia falciforme
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Mutação Glu6 Valna cadeia beta
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relaxado
Depois de contração “isotônica”- sarcômero fica menor (mais curta)- comprimento da banda A fica igual- banda I fica menor- aumenta a zona de superposição na banda A
O sarcômero
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Filamento fino (actina)
Filamento grosso(miosina)
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MIOSINA-uma proteína hexamérica(HL1L2)2
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Domínio motor da miosina-liga e hidrolisa ATP-liga a actina
Cadeias leves
Cadeiapesada
Sitio para ligarATP
Sitio paraligaractina
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Filamento grosso-baseado em miosina-bipolar
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Filamento fino-baseado em actina-polar
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