Measurement of Slow (μs−ms) Time Scale Dynamics in Protein Side Chains by 15N Relaxation Dispersion NMR Spectroscopy: Application to Asn and Gln Residues in a Cavity Mutant of T4 Lysozyme-Reference-Cited by-同舟云学术

Measurement of Slow (μs−ms) Time Scale Dynamics in Protein Side Chains by 15N Relaxation Dispersion NMR Spectroscopy: Application to Asn and Gln Residues in a Cavity Mutant of T4 Lysozyme

Published:2001-01-16 Issue:5 Volume:123 Page:967-975
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Mulder Frans A. A.¹,Skrynnikov Nikolai R.¹,Hon Bin¹,Dahlquist Frederick W.¹,Kay Lewis E.¹

Affiliation:

1. Contribution from the Protein Engineering Network Centres of Excellence and Departments of Medical Genetics, Biochemistry and Chemistry, University of Toronto, Toronto, Ontario, M5S 1A8 Canada, and Institute of Molecular Biology and Department of Chemistry, University of Oregon, Eugene, Oregon, 97403

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja003447g

Reference69 articles.

1. Conformational Substates in Proteins

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