Quantitative Analysis of Protein Unfolded State Energetics: Experimental and Computational Studies Demonstrate That Non-Native Side-Chain Interactions Stabilize Local Native Backbone Structure-Reference-Cited by-同舟云学术

Quantitative Analysis of Protein Unfolded State Energetics: Experimental and Computational Studies Demonstrate That Non-Native Side-Chain Interactions Stabilize Local Native Backbone Structure

Published:2021-03-29 Issue:13 Volume:125 Page:3269-3277
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Zou Junjie¹²,Xiao Shifeng³^ORCID,Simmerling Carlos¹²^ORCID,Raleigh Daniel P.¹²^ORCID

Affiliation:

1. Department of Chemistry, Stony Brook University, Stony Brook, New York 11794-3400, United States

2. Laufer Center for Physical and Quantitative Biology, Stony Brook University, Stony Brook, New York 11794-3400, United States

3. Shenzhen Key Laboratory of Marine Biotechnology and Ecology, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen 518060, China

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.0c08922

Reference74 articles.

1. NMR structure of the 35-residue villin headpiece subdomain

2. Dynamic NMR Line-Shape Analysis Demonstrates that the Villin Headpiece Subdomain Folds on the Microsecond Time Scale

3. Effect of modulating unfolded state structure on the folding kinetics of the villin headpiece subdomain

4. Common Structural Transitions in Explicit-Solvent Simulations of Villin Headpiece Folding

5. Rational Design, Structural and Thermodynamic Characterization of a Hyperstable Variant of the Villin Headpiece Helical Subdomain

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