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chaperonin
Chaperonins are proteins that provide favourable conditions for the correct folding of other proteins, thus preventing aggregation. Newly made proteins usually must fold from a linear chain of amino acids into a three-dimensional form. Chaperonins belong to a large class of molecules that assist protein folding, called molecular chaperones.〔(Howard Hughes Investigators: Arthur L. Horwich, M.D. )〕 The energy to fold proteins is supplied by adenosine triphosphate (ATP).
==Structure==
The structure of these chaperonins resemble two donuts stacked on top of one another to create a barrel.
Each ring is composed of either 7, 8 or 9 subunits depending on the organism in which the chaperonin is found.
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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