Side Chain Dynamics in Unfolded Protein States: an NMR Based 2H Spin Relaxation Study of Δ131Δ-Reference-Cited by-同舟云学术

Side Chain Dynamics in Unfolded Protein States: an NMR Based 2H Spin Relaxation Study of Δ131Δ

Published:2003-01-25 Issue:7 Volume:125 Page:1748-1758
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Choy Wing-Yiu¹,Shortle David¹,Kay Lewis E.¹

Affiliation:

1. Contribution from The Protein Engineering Network Center of Excellence and Departments of Medical Genetics and Microbiology, Biochemistry, and Chemistry, University of Toronto, Toronto, Ontario, Canada M5S 1A8 and Department of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja021179b

Reference74 articles.

1. Deuterium Spin Probes of Side-Chain Dynamics in Proteins. 1. Measurement of Five Relaxation Rates per Deuteron in 13C-Labeled and Fractionally 2H-Enriched Proteins in Solution

2. Coupling of folding and binding for unstructured proteins

3. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm

4. Natively unfolded proteins: A point where biology waits for physics

5. Intrinsically disordered protein

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