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PROTEIN FOLDING (CHAPERONINS (they have names: procaryots - GroES + GroEL,…
PROTEIN FOLDING
MOLECULAR CHAPERONS
non folded proteins so primary structure proteins can be aggregated by itselfs; molecular chaperons are proteins that prevent that when they are binded to proteins primary structure
CHAPERONINS
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they have names: procaryots - GroES + GroEL, eucaryots Tri C
GroES consist of 2 oligomer rings of 8 subunits and forms together with GroEL one whole protein; they form two sites - relaxed side of protein releasing and tight side where 2 subunits are interacted; they form also a small pocket where proteins can be sequesterede and so folded correctly under hydrolysis of ATP
TriC functions or rathe may function same, but it isnt known so goog ourdays as function of GroES
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SEQUENZ DETERMINES STRUCTURE, STRUCTURE DETERMINES FUNCTIONS