Collective NMR relaxation model applied to protein dynamics
- 7 February 1994
- journal article
- research article
- Published by American Physical Society (APS) in Physical Review Letters
- Vol. 72 (6) , 940-943
- https://doi.org/10.1103/physrevlett.72.940
Abstract
A new dynamical model for the interpretation of nuclear magnetic resonance relaxation data is presented. It is based on a normal mode description, treating the low frequencies associated with collective motions as adjustable parameters to optimize agreement between calculated and experimental relaxation order parameters. This model provides a compact representation of many aspects of internal dynamics and characterizes motions affecting different spin pairs in a correlated way. Furthermore, it links together dynamical characteristics of different types of NMR observables and allows one to assess vibrational thermodynamic properties. Sample applications are given for a 25-residue zinc-finger peptide.Keywords
This publication has 13 references indexed in Scilit:
- NMR relaxation and protein mobilityCurrent Opinion in Structural Biology, 1993
- Molecular dynamics analysis of NMR relaxation in a zinc-finger peptideJournal of the American Chemical Society, 1992
- Normal modes and NMR order parameters in proteinsJournal of the American Chemical Society, 1992
- Normal mode refinement: Crystallographic refinement of protein dynamic structure: I. Theory and test by simulated diffraction dataJournal of Molecular Biology, 1992
- Influence of vibrational motion on solid state line shapes and NMR relaxationThe Journal of Chemical Physics, 1985
- Protein normal-mode dynamics: Trypsin inhibitor, crambin, ribonuclease and lysozymeJournal of Molecular Biology, 1985
- Evaluation of the configurational entropy for proteins: application to molecular dynamics simulations of an α-helixMacromolecules, 1984
- Harmonic dynamics of proteins: normal modes and fluctuations in bovine pancreatic trypsin inhibitor.Proceedings of the National Academy of Sciences, 1983
- Dynamics of Native Globular Proteins in Terms of Dihedral AnglesJournal of the Physics Society Japan, 1983
- Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validityJournal of the American Chemical Society, 1982