Comparison of Methyl Rotation Axis Order Parameters Derived from Model-Free Analyses of 2H and 13C Longitudinal and Transverse Relaxation Rates Measured in the Same Protein Sample-Reference-Cited by-同舟云学术

Comparison of Methyl Rotation Axis Order Parameters Derived from Model-Free Analyses of 2H and 13C Longitudinal and Transverse Relaxation Rates Measured in the Same Protein Sample

Published:2001-05-30 Issue:25 Volume:123 Page:6164-6171
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Ishima Rieko¹,Petkova Aneta P.¹,Louis John M.¹,Torchia Dennis A.¹

Affiliation:

1. Contribution from the Molecular Structural Biology Unit, National Institute of Dental and Craniofacial Research, and the Laboratory of Chemical Physics, National Institutes of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja0104711

Reference41 articles.

1. THEORY AND PRACTICE OF NUCLEAR SPIN RELAXATION IN PROTEINS

2. Nicholson, L. K.; Kay, L. E.; Torchia, D. A.Protein Dynamics asStudied by Solution NMR Techniques; Sarkar, S. K., Ed.; Elsevier: Amsterdam, 1996; pp 241−279.

3. Molecular Dynamics of Staphylococcal Nuclease: Comparison of Simulation with 15N and 13C NMR Relaxation Data

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