The Use of Residual Dipolar Coupling in Concert with Backbone Relaxation Rates to Identify Conformational Exchange by NMR
- 14 April 1999
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 121 (17), 4282-4283
- https://doi.org/10.1021/ja990062t
Abstract
No abstract availableThis publication has 10 references indexed in Scilit:
- Using Amide 1H and 15N Transverse Relaxation To Detect Millisecond Time-Scale Motions in Perdeuterated Proteins: Application to HIV-1 ProteaseJournal of the American Chemical Society, 1998
- Longitudinal and Transverse 1H−15N Dipolar/15N Chemical Shift Anisotropy Relaxation Interference: Unambiguous Determination of Rotational Diffusion Tensors and Chemical Exchange Effects in Biological MacromoleculesJournal of the American Chemical Society, 1998
- Measurement ofJand Dipolar Couplings from Simplified Two-Dimensional NMR SpectraJournal of Magnetic Resonance, 1998
- Direct Measurement of Distances and Angles in Biomolecules by NMR in a Dilute Liquid Crystalline MediumScience, 1997
- Monitoring Macromolecular Motions on Microsecond to Millisecond Time Scales by R1ρ−R1 Constant Relaxation Time NMR SpectroscopyJournal of the American Chemical Society, 1996
- Magnetically-oriented phospholipid micelles as a tool for the study of membrane-associated moleculesProgress in Nuclear Magnetic Resonance Spectroscopy, 1994
- Study of Protein Dynamics by NMRPublished by Springer Nature ,1993
- Heteronuclear NMR Studies of the Molecular Dynamics of Staphylococcal NucleasePublished by Springer Nature ,1993
- Characterization of magnetically orientable bilayers in mixtures of dihexanoylphosphatidylcholine and dimyristoylphosphatidylcholine by solid-state NMRBiochemistry, 1992
- Backbone dynamics of calmodulin studied by nitrogen-15 relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexibleBiochemistry, 1992