Conformation and Thermal Denaturation of Apocalmodulin: Role of Electrostatic Mutations-Reference-Cited by-同舟云学术

Conformation and Thermal Denaturation of Apocalmodulin: Role of Electrostatic Mutations

Published:1997-02-01 Issue:8 Volume:36 Page:2017-2024
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Protasevich Irina¹,Ranjbar Bijan¹,Lobachov Vladimir¹,Makarov Alexander¹,Gilli Robert¹,Briand Claudette¹,Lafitte Daniel¹,Haiech Jacques¹

Affiliation:

1. Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov Street 32, 117984 Moscow, Russia, Faculte de Pharmacie, URA CNRS 1924, Bd Jean Moulin 27, 13385 Marseille Cedex 5, France, and Laboratoire de Chimie Bacterienne, UPR 7221, CNRS, Chemin J. Aiguier 31, 13009 Marseille, France

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi962538g

Reference45 articles.

1. Investigating the High Affinity and Low Sequence Specificity of Calmodulin Binding to its Targets

2. Low frequency variability and interstellar focusing

3. The α-helical content of calmodulin is increased by solution conditions favouring protein crystallisation

4. Calmodulin structure refined at 1.7 Å resolution

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