Analysis of Internally Restricted Correlated Rotations in Peptides and Proteins Using 13C and 15N NMR Relaxation Data
- 1 January 1996
- journal article
- research article
- Published by American Chemical Society (ACS) in The Journal of Physical Chemistry
- Vol. 100 (20) , 8378-8388
- https://doi.org/10.1021/jp9531927
Abstract
No abstract availableKeywords
This publication has 18 references indexed in Scilit:
- NMR solution structure of the 32-kDa platelet factor 4 ELR-motif N-terminal chimera: a symmetric tetramerBiochemistry, 1995
- Peptide Dynamics in Triglycine: Coupling of Internal Bond Rotations and Overall Molecular TumblingThe Journal of Physical Chemistry, 1994
- Normal mode analysis of protein dynamicsCurrent Opinion in Structural Biology, 1994
- Carbon-13 nuclear magnetic resonance relaxation-derived .psi., .PHI. bond rotational energy barriers and rotational restrictions for glycine 13C.alpha.-methylenes in a GXX-repeat hexadecapeptideBiochemistry, 1993
- Large-amplitude nonlinear motions in proteinsPhysical Review Letters, 1992
- Spin-lattice relaxation of coupled nuclear spins with applications to molecular motion in liquidsChemical Reviews, 1991
- Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteinsJournal of the American Chemical Society, 1990
- Nuclear magnetic spin relaxation of a spin-pair undergoing reorientations by jumping among unequivalent sitesMolecular Physics, 1979
- Calculated carbon-13 NMR relaxation parameters for a restricted internal diffusion model. Application to methionine relaxation in dihydrofolate reductaseJournal of the American Chemical Society, 1978
- Dynamics of folded proteinsNature, 1977