Quantification of Drive-Response Relationships Between Residues During Protein Folding
Author:
Affiliation:
1. Department of Molecular Biosciences and Center for Bioinformatics, The University of Kansas, 2030 Becker Drive, Lawrence, Kansas 66047, United States
Publisher
American Chemical Society (ACS)
Subject
Physical and Theoretical Chemistry,Computer Science Applications
Link
https://pubs.acs.org/doi/pdf/10.1021/ct4002784
Reference39 articles.
1. Protein aggregation determinants from a simplified model: Cooperative folders resist aggregation
2. Prevention of amyloid‐like aggregation as a driving force of protein evolution
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4. Correlated dynamics of consecutive residues reveal transient and cooperative unfolding of secondary structure in proteins
5. Functional dynamics of proteins revealed by solution NMR
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