title: Unraveling protein dynamics through fast spectral density mapping.
abstract: Spectral density mapping at multiple NMR field strengths is probably the best method to describe the dynamical behavior of a protein in solution through the analysis of 15N heteronuclear relaxation parameters. Nevertheless, such analyses are scarcely reported in the literature, probably because this method is excessively demanding in spectrometer measuring time. Indeed, when using n different magnetic fields and assuming the validity of the high frequency approximation, the discrete sampling of the spectral density function with 2n + 1 points needs the measurement of 3n 15N heteronuclear relaxation measurements (n R1, n R2, and n15N{1H}NOEs). Based on further approximations, we proposed a new strategy that allows us to describe the spectral density with n + 2 points, with the measurement of a total of n + 2 heteronuclear relaxation parameters. Applied to the dynamics analysis of the protein p13( MTCP1) at three different NMR fields, this approach allowed us to divide by nearly a factor of two the total measuring time, without altering further results obtained by the "model free" analysis of the resulting spectral densities. Furthermore, simulations have shown that this strategy remains applicable to any low isotropically tumbling protein (tauc>3 ns), and is valid for the types of motion generally envisaged for proteins.
authors.affiliation: Centre de Biochimie Structurale, UMR UM1/5048 CNRS/554 INSERM, 29 rue de Navacelles, 34090, Montpellier Cedex, France.
authors.forename: Virginie
authors.initials: V
authors.lastname: Ropars
authors.forename: Sabine
authors.initials: S
authors.lastname: Bouguet-Bonnet
authors.forename: Daniel
authors.initials: D
authors.lastname: Auguin
authors.forename: Philippe
authors.initials: P
authors.lastname: Barthe
authors.forename: Daniel
authors.initials: D
authors.lastname: Canet
authors.forename: Christian
authors.initials: C
authors.lastname: Roumestand
mesh_terms: D001703:Biophysics / Q000379:methods; D003198:Computer Simulation; D006801:Humans; D015233:Models, Statistical; D008968:Molecular Conformation; D009587:Nitrogen Isotopes / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010539:Permeability; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D011518:Proto-Oncogene Proteins / Q000737:chemistry; D013053:Spectrophotometry / Q000379:methods
chemical_list: C082870:MTCP1 protein, human; D009587:Nitrogen Isotopes; D011506:Proteins; D011518:Proto-Oncogene Proteins