Influence of temperature and denaturing agents on the structural stability of calmodulin

FEBS Letters

Guerini, Danilo¹  Krebs, Joachim¹ 

[1] Laboratory of Biochemistry, Swiss Federal Institute of Technology (ETH), Universitätsstr. 16, CH-8092 Zürich, Switzerland

关键词: Calmodulin;    Structural stability;    Calmodulin denaturation;    Nuclear magnetic resonance;   

DOI  :  10.1016/0014-5793(83)80029-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The structural stability of calmodulin was studied by ¹H-nuclear magnetic resonance spectroscopy under different denaturing conditions. The presence of Ca²⁺ stabilizes the structural properties of the native protein. In the absence of calcium the structural integrity of calmodulin can easily be affected by elevated temperatures or by high concentrations of denaturing agents. The unfolding process under various denaturing conditions is reversible underlining the high degree of structural flexibility of this protein.

【 授权许可】

Unknown