期刊
PROTEIN SCIENCE
卷 16, 期 11, 页码 2334-2344出版社
WILEY
DOI: 10.1110/ps.073164107
关键词
intrinsically disordered proteins; nucleation; oligomers; polymerization; fluorescence spectroscopy; NMR
资金
- NIDDK NIH HHS [DK 13332, R01 DK013332] Funding Source: Medline
Amyloid formation typically follows a time course in which there is a long lag period followed by a rapid formation of fibrils. In this review, I show that the standard mechanisms of polymerization need to be expanded to consider that the monomeric proteins/peptides involved in amyloid formation are intrinsically disordered and exist as an ensemble of disordered-collapsed states. The review focuses primarily on events which occur in the long lag period defining these as protein folding issues, coupled with formation of oligomers. Experimental methods to explore folding and oligomerization issues over a wide range of protein concentrations using primarily fluorescence and F-19-NMR methods are discussed.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据