A Theory of Protein Dynamics to Predict NMR Relaxation
- 15 December 2007
- journal article
- Published by Elsevier in Biophysical Journal
- Vol. 93 (12), 4128-4140
- https://doi.org/10.1529/biophysj.107.111849
Abstract
No abstract availableKeywords
Funding Information
- American Chemical Society Petroleum Research Fund
- National Science Foundation (0509808)
This publication has 56 references indexed in Scilit:
- Characterization of the Fast Dynamics of Protein Amino Acid Side Chains Using NMR Relaxation in SolutionChemical Reviews, 2006
- Reconciling the “old” and “new” views of protein allostery: A molecular simulation study of chemotaxis Y protein (CheY)Proteins-Structure Function and Bioinformatics, 2006
- GROMACS: Fast, flexible, and freeJournal of Computational Chemistry, 2005
- Vibrational Dynamics of Folded Proteins: Significance of Slow and Fast Motions in Relation to Function and StabilityPhysical Review Letters, 1998
- Contributions to protein entropy and heat capacity from bond vector motions measured by NMR spin relaxationJournal of Molecular Biology, 1997
- Contributions to Conformational Entropy Arising from Bond Vector Fluctuations Measured from NMR-Derived Order Parameters: Application to Protein FoldingJournal of Molecular Biology, 1996
- A 500 ps molecular dynamics simulation study of interleukin-1β in water: Correlation with nuclear magnetic resonance spectroscopy and crystallographyJournal of Molecular Biology, 1992
- Interior and surface of monomeric proteinsJournal of Molecular Biology, 1987
- Viscoelastic relaxation of segment orientation in dilute polymer solutions. II. Stiffness dependence of fluorescence depolarizationThe Journal of Chemical Physics, 1986
- Optimized Rouse–Zimm theory for stiff polymersThe Journal of Chemical Physics, 1978