An Approach to Direct Determination of Protein Dynamics from 15N NMR Relaxation at Multiple Fields, Independent of Variable 15N Chemical Shift Anisotropy and Chemical Exchange Contributions
- 1 September 1999
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 121 (37) , 8577-8582
- https://doi.org/10.1021/ja9904991
Abstract
No abstract availableThis publication has 14 references indexed in Scilit:
- The Use of Residual Dipolar Coupling in Concert with Backbone Relaxation Rates to Identify Conformational Exchange by NMRJournal of the American Chemical Society, 1999
- Contributions to Conformational Entropy Arising from Bond Vector Fluctuations Measured from NMR-Derived Order Parameters: Application to Protein FoldingJournal of Molecular Biology, 1996
- Monitoring Macromolecular Motions on Microsecond to Millisecond Time Scales by R1ρ−R1 Constant Relaxation Time NMR SpectroscopyJournal of the American Chemical Society, 1996
- Simultaneous Characterization of the Amide 1H Chemical Shift, 1H-15N Dipolar, and 15N Chemical Shift Interaction Tensors in a Peptide Bond by Three-Dimensional Solid-State NMR SpectroscopyJournal of the American Chemical Society, 1995
- Backbone dynamics of ribonuclease T1 and its complex with 2?GMP studied by two-dimensional heteronuclear NMR spectroscopyJournal of Biomolecular NMR, 1994
- NMR order parameters and free energy: an analytical approach and its application to cooperative calcium(2+) binding by calbindin D9kJournal of the American Chemical Society, 1993
- 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
- Nitrogen-15 NMR chemical shift tensors and conformation of some nitrogen-15-labeled polypeptides in the solid stateMacromolecules, 1989
- Determination of the nitrogen-15 and carbon-13 chemical shift tensors of L-[13C]alanyl-L-[15N]alanine from the dipole-coupled powder patternsJournal of the American Chemical Society, 1987
- The amide nitrogen-15 chemical shift tensors of four peptides determined from carbon-13 dipole-coupled chemical shift powder patternsJournal of the American Chemical Society, 1987