Denatured-State Ensemble and the Early-Stage Folding of the G29A Mutant of the B-Domain of Protein A
Author:
Affiliation:
1. University of CaliforniaDavis Genome Center and Bioinformatics Program, Department of Applied Science, University of California, One Shields Avenue, Davis, California 95616
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/jp0449814
Reference49 articles.
1. NMR Determination of Residual Structure in a Urea-Denatured Protein, the 434-Repressor
2. High populations of non-native structures in the denatured state are compatible with the formation of the native folded state
3. Structural Characterization of Folded and Unfolded States of an SH3 Domain in Equilibrium in Aqueous Buffer
4. Similarities between the spectrin SH3 domain denatured state and its folding transition state11Edited by A. R. Fersht
5. Native-like Mean Structure in the Unfolded Ensemble of Small Proteins
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