Nonexponential Kinetics of Loop Formation in Proteins and Peptides: A Signature of Rugged Free Energy Landscapes?
Author:
Affiliation:
1. Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, U.K.
2. Institute of Macromolecular Compounds of Russian Academy of Sciences, St. Petersburg, Russia
Funder
Wellcome Trust
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.7b07075
Reference39 articles.
1. Role of Backbone−Solvent Interactions in Determining Conformational Equilibria of Intrinsically Disordered Proteins
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3. Structural Ensemble of an Intrinsically Disordered Polypeptide
4. Fast events in protein folding initiated by nanosecond laser photolysis.
5. The speed limit for protein folding measured by triplet-triplet energy transfer
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