收稿日期: 2002-01-29
网络出版日期: 2002-03-18
基金资助
supportedbyPandengProjectoftheChineseMinistryofScienecandTechnology;973 project(G19990 75 60 8)
Effects of Molecular Chaperone, Protein Aggregation and Macromolecular Crowding on Protein Folding
Received date: 2002-01-29
Online published: 2002-03-18
李剑 , 王志珍 . 分子伴侣、蛋白质聚集和大分子拥挤环境对蛋白质折叠的影响(英)[J]. 中国科学院大学学报, 2002 , 19(2) : 215 -218 . DOI: 10.7523/j.issn.2095-6134.2002.2.021
The effects of molecular chaperones, protein aggregation and macromolecular crowding on protein folding have been studied. It has been demonstrated that there are two binding ways between molecular chaperone GroEL and its substrates, "all of sites" and "half of sites", depending on the shape, the size of substrates and the interaction between GroEL and substrates. It has also provided insights into a mechanism of cells to prevent protein folding against interference from aggregation of other proteins. In addition, it has been suggested that pre-molten globule state of α-lactalbumin is the target not only for chaperones but also for protein aggregates. Finally, it has displayed the complexity and the diversity of effects of macromolecular crowding on both the thermodynamics and kinetics of protein folding and assembly.
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