title: Protein dynamics from a NMR perspective: networks of coupled rotators and fractional Brownian dynamics.
abstract: Nuclear magnetic resonance (NMR) has proven to be the most valuable tool for investigating internal dynamics of proteins. In this perspective, the interpretation of NMR relaxation data eventually relies on a model of the motions. In this article, we propose to compare two radically different approaches that aim at describing internal dynamics in proteins. It is shown that the correlation functions predicted by a network of coupled rotators can be interpreted in terms of a heuristic approach based on fractional Brownian dynamics for each of the vectors in the network. Our results are interpreted in terms of the probability distributions of relaxation modes in both processes, the median of which turns out to be the relevant quantity for the comparison of both models.
authors.affiliation: Centre de Biophysique Moléculaire, CNRS, Rue Charles Sadron, 45071 Orléans, France. vania.calandrini@cnrs-orleans.fr
authors.forename: Vania
authors.initials: V
authors.lastname: Calandrini
authors.forename: Daniel
authors.initials: D
authors.lastname: Abergel
authors.forename: Gerald R
authors.initials: GR
authors.lastname: Kneller
mesh_terms: D003198:Computer Simulation; D004058:Diffusion; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008956:Models, Chemical; D008958:Models, Molecular; D015233:Models, Statistical; D008968:Molecular Conformation; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D009038:Motion; D046912:Multiprotein Complexes / Q000737:chemistry / Q000648:ultrastructure
chemical_list: D020409:Molecular Motor Proteins; D046912:Multiprotein Complexes