Analysis of Slow Interdomain Motion of Macromolecules Using NMR Relaxation Data-Reference-Cited by-同舟云学术

Analysis of Slow Interdomain Motion of Macromolecules Using NMR Relaxation Data

Published:2001-03-31 Issue:17 Volume:123 Page:3953-3959
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Baber James L.¹,Szabo Attila¹,Tjandra Nico¹

Affiliation:

1. Contribution from the Laboratory of Biophysical Chemistry, Building 3, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892-0380, and Laboratory of Chemical Physics, National Institute 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/ja0041876

Reference36 articles.

1. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results

2. Backbone dynamics of calmodulin studied by nitrogen-15 relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible

3. The 1.0 Å crystal structure of Ca2+-bound calmodulin: an analysis of disorder and implications for functionally relevant plasticity

4. Calcium-induced increase in the radius of gyration and maximum dimension of calmodulin measured by small-angle x-ray scattering

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