Nonnative Interactions in the FF Domain Folding Pathway from an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study-Reference-Cited by-同舟云学术

Nonnative Interactions in the FF Domain Folding Pathway from an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study

Published:2011-06-28 Issue:28 Volume:133 Page:10974-10982
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Korzhnev Dmitry M.¹²,Vernon Robert M.³,Religa Tomasz L.¹,Hansen Alexandar L.¹,Baker David³,Fersht Alan R.⁴,Kay Lewis E.¹

Affiliation:

1. Departments of Molecular Genetics, Biochemistry and Chemistry, The University of Toronto, Toronto, Ontario M5S 1A8, Canada

2. Department of Molecular, Microbial and Structural Biology, University of Connecticut Health Center, Farmington, Connecticut 06030, United States

3. Department of Biochemistry, University of Washington, Box 357350, 1705 NE Pacific Street, Seattle, Washington 98195-7350, United States

4. Center for Protein Engineering, Medical Research Council, Cambridge, United Kingdom

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja203686t

Reference41 articles.

1. Mapping the transition state and pathway of protein folding by protein engineering

2. Topological and energetic factors: what determines the structural details of the transition state ensemble and “en-route” intermediates for protein folding? an investigation for small globular proteins

3. Intermediates: ubiquitous species on folding energy landscapes?

4. A protein folding pathway with multiple folding intermediates at atomic resolution

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