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
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