ENERGETICS OF PROTEIN-STRUCTURE AND FOLDING
ENERGETICS OF PROTEIN-STRUCTURE AND FOLDING
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DOI：
10.1002/bip.360240114
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发表时间：
1985-01-01
期刊：
影响因子：
2.9
通讯作者：
CREIGHTON, TE
中科院分区：
文献类型：
--
作者：
GOLDENBERG, DP;CREIGHTON, TE
综述了小分子蛋白质去折叠和重折叠动力学的实验数据。排除由于肽键的顺式-反式异构化引起的未折叠蛋白质中的缓慢转变，可以得出结论，未折叠和重折叠中的速率限制过渡态是完全折叠状态的高能扭曲。部分折叠的中间体对于折叠无疑是重要的，但它们的形成通常不受速率限制。一个简单的模型被用来说明蛋白质折叠能量学的一些方面。
The available experimental date on the kinetics of unfolding and refolding of small proteins are reviewed. Excluding slow transitions in the unfolded protein due tocis–transisomerization of peptide bonds, the rate‐limiting transition state in both unfolding and refolding is concluded to be a high‐energy distortion of the fully folded state. Partially folded intermediates are undoubtedly important for folding, but their formation is normally not rate limiting. A simple model is used to illustrate some of the aspects of protein‐folding energetics.