寡聚酶的折叠与缔合
Folding and association of oligomeric enzymes.
作者信息
Jaenicke R
出版信息
Naturwissenschaften. 1978 Nov;65(11):569-77. doi: 10.1007/BF00364906.
PMID:732881
Abstract
The spontaneous structure formation of oligomeric enzymes consists of the consecutive 'folding' and association of the constituent polypeptide chains. Whether catalytic function is an intrinsic property of the folded monomers may be determined using kinetic reconstitution experiments. It is shown that full activity requires association; the correct assembly of subunits depends on their proper folding. The native structure is determined as the kinetically accessible state of lowest free energy.
摘要
寡聚酶的自发结构形成由组成多肽链的连续“折叠”和缔合组成。催化功能是否是折叠单体的固有属性可以通过动力学重组实验来确定。结果表明，完全活性需要缔合；亚基的正确组装取决于它们的正确折叠。天然结构被确定为最低自由能的动力学可及状态。
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