The Length of the Calmodulin Linker Determines the Extent of Transient Interdomain Association and Target Affinity-Reference-Cited by-同舟云学术

The Length of the Calmodulin Linker Determines the Extent of Transient Interdomain Association and Target Affinity

Published:2013-06-20 Issue:26 Volume:135 Page:9648-9651
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Anthis Nicholas J.¹,Clore G. Marius¹

Affiliation:

1. Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, United States

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja4051422

Reference17 articles.

1. Calcium-induced conformational transition revealed by the solution structure of apo calmodulin

2. Calmodulin's Flexibility Allows for Promiscuity in Its Interactions with Target Proteins and Peptides

3. Solution structure of a calmodulin-target peptide complex by multidimensional NMR

4. Target Enzyme Recognition by Calmodulin: 2.4 Å Structure of a Calmodulin-Peptide Complex

5. Three-dimensional structure of calmodulin

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