Binding and backbone dynamics of protein under topological constraint: calmodulin as a model system-Reference-Cited by-同舟云学术

Binding and backbone dynamics of protein under topological constraint: calmodulin as a model system

Published:2018 Issue:64 Volume:54 Page:8917-8920
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Katyal Priya¹²³⁴,Yang Yongkun⁵⁶²³⁴,Fu You-Jun⁷²³⁴,Iandosca Jennifer⁵⁶²³⁴,Vinogradova Olga¹²³⁴,Lin Yao⁵⁶²³⁴^ORCID

Affiliation:

1. Department of Pharmaceutical Sciences

2. University of Connecticut

3. Storrs

4. USA

5. Polymer Program

6. Institute of Materials Science

7. Department of Chemistry

Abstract

Using calmodulin as a model system, we present the possible effect of topological constraint on protein backbone dynamics and binding thermodynamics.

Funder

U.S. Department of Education

Alexander von Humboldt-Stiftung

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2018/CC/C8CC03977A

Reference35 articles.

1. The role of conformational entropy in molecular recognition by calmodulin

2. Genetic polymorphism and protein conformational plasticity in the calmodulin superfamily: Two ways to promote multifunctionality

3. Structure of calmodulin refined at 2.2 Å resolution

4. Three-dimensional structure of calmodulin

5. Calmodulin structure refined at 1.7 Å resolution

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