Proline cis-trans isomerization and protein folding
Proline cis-trans isomerization and protein folding
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DOI：
10.1021/bi020574b
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发表时间：
2002-12-17
期刊：
影响因子：
2.9
通讯作者：
Scheraga, HA
中科院分区：
文献类型：
--
作者：
Wedemeyer, WJ;Welker, E;Scheraga, HA
脯氨酸顺反异构化在蛋白质折叠的速率决定步骤中起关键作用。本文总结了这一异构化过程的能量起源，并以二硫化物完整的牛胰腺核糖核酸酶A的折叠和展开为例，说明了从异质展开状态（由X-Pro肽基团的顺式和反式异构体组成）到仅存在一组脯氨酸异构体的天然结构的构象变化的动力学和结构特征。
Proline cis-trans isomerization plays a key role in the rate-determining steps of protein folding. The energetic origin of this isomerization process is summarized, and the folding and unfolding of disulfide-intact bovine pancreatic ribonuclease A is used as an example to illustrate the kinetics and structural features of conformational changes from the heterogeneous unfolded state (consisting of cis and trans isomers of X-Pro peptide groups) to the native structure in which only one set of proline isomers is present.