Kinesis of polypeptide during GroEL-mediated folding
Kinesis of polypeptide during GroEL-mediated folding
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DOI：
10.1101/sqb.1995.060.01.048
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发表时间：
1995-01-01
期刊：
影响因子：
--
通讯作者：
Fenton, WA
中科院分区：
文献类型：
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作者：
Horwich, AL;Weissman, JS;Fenton, WA
被称为伴侣蛋白的大双环结构促进大量新合成和新易位的多肽依赖 ATP 折叠成天然形式的机制一直是蛋白质运动一般领域中备受关注的主题。最近对细菌伴侣蛋白 GroEL 的结构和功能研究已经开始了解这一过程，特别是传达有关在此类反应期间蛋白质底物发生的情况的信息。在这里，我们总结了这些发现并讨论了它们的含义，并考虑了尚未解决的问题，以及未来实验的可能目标。
The mechanism by which the large double-ring structures known as chaperonins facilitate the ATP-dependent folding to native form of a large number of newly synthesized and newly translocated polypeptides has been a subject of considerable interest in the general area of protein kinesis. Recent structural and functional studies of the bacterial chaperonin GroEL have begun to inform on this process, in particular conveying information on what happens to the protein substrate during such a reaction. Here we summarize these findings and discuss their implications, and also consider issues that remain unsettled, likely targets of future experimentation.