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Default Temperature dependence of NMR order parameters and protein dynamics.

Temperature dependence of NMR order parameters and protein dynamics.

Related Articles Temperature dependence of NMR order parameters and protein dynamics.

J Am Chem Soc. 2003 Sep 17;125(37):11158-9

Authors: Massi F, Palmer AG

The helical subdomain, HP36, of the F-actin-binding headpiece domain of chicken villin, is the smallest naturally occurring polypeptide that folds to a thermostable compact structure. Unconstrained molecular dynamics simulations and constrained molecular dynamics simulations using umbrella sampling are used to study the temperature dependence of internal motions of the backbone amide moieties of HP36. The potential of mean force (PMF) for the N-H bond vector, determined from the constrained simulations, is found to be temperature dependent. A simple analytical expression is derived that describes the temperature dependence of the PMF. The parameters of this model are obtained from the PMF, from the unconstrained molecular dynamics simulations, or from experimental values of the generalized order parameter. The results provide a linkage between experimental and theoretical measures of the temperature dependence of protein motions.

PMID: 16220912 [PubMed - indexed for MEDLINE]



Source: PubMed
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