Biophysical Study of Thermal Denaturation of Apo-calmodulin: Dynamics of Native and Unfolded States

Overview

Journal Biophys J

Publisher Cell Press

Specialty Biophysics

Date 2008 Jan 29

PMID 18223007

Citations 7

Authors

Gabriel Gibrat

France Liliane Assairi

Yves Blouquit

Constantin T Craescu

Marie-Claire Bellissent-Funel

Affiliations

Soon will be listed here.

Abstract

Apo-calmodulin, a small, mainly alpha, soluble protein is a calcium-dependent protein activator. This article presents a study of internal dynamics of native and thermal unfolded apo-calmodulin, using quasi-elastic neutron scattering. This technique can probe protein internal dynamics in the picosecond timescale and in the nanometer length-scale. It appears that a dynamical transition is associated with thermal denaturation of apo-calmodulin. This dynamical transition goes together with a decrease of the confinement of hydrogen atoms, a decrease of immobile protons proportion and an increase of dynamical heterogeneity. The comparison of native and unfolded states dynamics suggests that the dynamics of protein atoms is more influenced by their distance to the backbone than by their solvent exposure.

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