Fractional protein dynamics seen by nuclear magnetic resonance spectroscopy: Relating molecular dynamics simulation and experiment. - Archive ouverte HAL
Article Dans Une Revue The Journal of Chemical Physics Année : 2010

Fractional protein dynamics seen by nuclear magnetic resonance spectroscopy: Relating molecular dynamics simulation and experiment.

Résumé

We propose a fractional Brownian dynamics model for time correlation functions characterizing the internal dynamics of proteins probed by NMR relaxation spectroscopy. The time correlation functions are represented by a broad distribution of exponential functions which are characterized by two parameters. We show that the model describes well the restricted rotational motion of N-H vectors in the amide groups of lysozyme obtained from molecular dynamics simulation and that reliable predictions of experimental relaxation rates can be obtained on that basis.

Domaines

Chimie organique
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Dates et versions

hal-00593171 , version 1 (13-05-2011)

Identifiants

Citer

Vania Calandrini, Daniel Abergel, Gerald R Kneller. Fractional protein dynamics seen by nuclear magnetic resonance spectroscopy: Relating molecular dynamics simulation and experiment.. The Journal of Chemical Physics, 2010, 133 (14), pp.145101. ⟨10.1063/1.3486195⟩. ⟨hal-00593171⟩
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