Experimental Characterization of Models for Backbone Picosecond Dynamics in Proteins. Quantification of NMR Auto- and Cross-correlation Relaxation Mechanisms Involving Different Nuclei of the Peptide Plane
- 1 December 1997
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 119 (51) , 12629-12642
- https://doi.org/10.1021/ja972083y
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- NMR Assignments, Secondary Structure and Hydration of Oxidized Escherichia coli FlavodoxinEuropean Journal of Biochemistry, 1997
- Monitoring Macromolecular Motions on Microsecond to Millisecond Time Scales by R1ρ−R1 Constant Relaxation Time NMR SpectroscopyJournal of the American Chemical Society, 1996
- Characterization of biomolecular structure and dynamics by NMR cross relaxationProgress in Nuclear Magnetic Resonance Spectroscopy, 1994
- Essential dynamics of proteinsProteins-Structure Function and Bioinformatics, 1993
- 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
- Ultraviolet resonance Raman study on the binding mode of enkephalin to phospholipid membranesJournal of the American Chemical Society, 1992
- Molecular Switch for Signal Transduction: Structural Differences Between Active and Inactive Forms of Protooncogenic ras ProteinsScience, 1990
- Conformational Substates in ProteinsAnnual Review of Biophysics, 1988
- 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
- Relaxation Processes in a System of Two SpinsPhysical Review B, 1955