Eliminating a Protein Folding Intermediate by Tuning a Local Hydrophobic Contact
Author:
Affiliation:
1. Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853-1301, United States
Funder
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.6b07250
Reference56 articles.
1. Amyloid fibril formation by an SH3 domain
2. A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro
3. Rapid amyloid fiber formation from the fast-folding WW domain FBP28
4. Folding, Misfolding, and Amyloid Protofibril Formation of WW Domain FBP28
5. Structure of an Intermediate State in Protein Folding and Aggregation
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