Calcium-induced changes in calmodulin structural dynamics and thermodynamics

  • Wu G
  • Gao Z
  • Dong A
 et al. 
  • 34


    Mendeley users who have this article in their library.
  • 19


    Citations of this article.


The thermodynamics of the interaction between Ca2+and calmodulin (CaM) was examined using isothermal titration calorimetry (ITC). The chemical denaturation of calmodulin was monitored spectroscopically to determine the stability of Ca2+-free (apo) and Ca2+-loaded (holo) CaMs. We explored the conformational and structural dynamics of CaM using amide hydrogen-deuterium (H-D) exchange coupled with Fourier transform infrared (FT-IR) spectroscopy. The results of H-D exchange and FT-IR suggest that CaM activation by Ca2+binding involves significant conformational changes. The results have also revealed that while the overall conformation of holo-CaM is more stable than that of the apo-CaM, some part of its α-helix structures, most likely the EF-hand domain region, has more solvent exposure, thus, has a faster H-D exchange rate than that of the apo-CaM. The ITC method provides a new strategy for obtaining site-specific Ca2+binding properties and a better estimation of the cooperativity and conformational change contributions of coupled EF-hand proteins. © 2012 Elsevier B.V.

Author-supplied keywords

  • CaM
  • Conformational change
  • Structural dynamics
  • Thermodynamics

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document


  • Guangrong Wu

  • Zhengya Gao

  • Aichun Dong

  • Shaoning Yu

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free