Probing protein folding and stability using disulfide bonds
Probing protein folding and stability using disulfide bonds
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DOI：
10.1007/bf02821544
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发表时间：
1997-02-01
影响因子：
2.6
通讯作者：
Creighton, TE
中科院分区：
文献类型：
--
作者：
Darby, N;Creighton, TE
二硫键是稳定许多蛋白质折叠构象所必需的。二硫键形成和断裂过程的速率和平衡可以通过实验来控制，并可用于获得有关蛋白质折叠和稳定性的重要信息。这里描述了一些研究这些过程的实验程序，以及解释所得数据的方法。
Disulfide bonds are required to stabilize the folded conformations of many proteins. The rates and equilibria Of processes involved in disulfide bond formation and breakage can be manipulated experimentally and can be used to obtain important information about protein folding and stability. A number of experimental procedures for studying these processes, and approaches to interpreting the resulting data, are described here.