Journal
PROTEIN SCIENCE
Volume 16, Issue 11, Pages 2334-2344Publisher
WILEY
DOI: 10.1110/ps.073164107
Keywords
intrinsically disordered proteins; nucleation; oligomers; polymerization; fluorescence spectroscopy; NMR
Categories
Funding
- NIDDK NIH HHS [DK 13332, R01 DK013332] Funding Source: Medline
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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.
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