Temperature Dependence of Domain Motions of Calmodulin Probed by NMR Relaxation at Multiple Fields-Reference-Cited by-同舟云学术

Temperature Dependence of Domain Motions of Calmodulin Probed by NMR Relaxation at Multiple Fields

Published:2003-08-22 Issue:37 Volume:125 Page:11379-11384
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Chang Shou-Lin¹,Szabo Attila¹,Tjandra Nico¹

Affiliation:

1. Contribution from the Laboratory of Biophysical Chemistry, Building 50, National Heart, Lung, and Blood Institute and Laboratory of Chemical Physics, National Institute of Diabetes, 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/ja034064w

Reference31 articles.

1. Cohen, P.; Klee, C. B.Calmodulin; Elsevier: 1988.

2. Carp Muscle Calcium-binding Protein

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

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

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