Analysis of the relationship between enzyme activity and its internal motion using nuclear magnetic resonance: 15N relaxation studies of wild-type and mutant lysozyme
- 12 March 1999
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 286 (5) , 1547-1565
- https://doi.org/10.1006/jmbi.1999.2572
Abstract
No abstract availableKeywords
Funding Information
- Ministry of Education, Culture, Sports, Science and Technology
This publication has 43 references indexed in Scilit:
- Backbone and Side Chain Dynamics of Uncomplexed Human Adipocyte and Muscle Fatty Acid-Binding ProteinsBiochemistry, 1998
- NMRPipe: A multidimensional spectral processing system based on UNIX pipesJournal of Biomolecular NMR, 1995
- Long-Range Motional Restrictions in a Multidomain Zinc-Finger Protein from Anisotropic TumblingScience, 1995
- Structural Determinants of Protein Dynamics: Analysis of 15N NMR Relaxation Measurements for Main-Chain and Side-Chain Nuclei of Hen Egg White LysozymeBiochemistry, 1995
- Refinement of an enzyme complex with inhibitor bound at partial occupancyJournal of Molecular Biology, 1992
- A common sense approach to peak picking in two-, three-, and four-dimensional spectra using automatic computer analysis of contour diagramsJournal of Magnetic Resonance (1969), 1991
- Analysis of the backbone dynamics of interleukin-1.beta. using two-dimensional inverse detected heteronuclear nitrogen-15-proton NMR spectroscopyBiochemistry, 1990
- Heteronuclear three-dimensional nmr spectroscopy. A strategy for the simplification of homonuclear two-dimensional NMR spectraJournal of Magnetic Resonance (1969), 1988
- Structure of a complex between yeast hexokinase A and glucoseJournal of Molecular Biology, 1980
- Crystallographic studies of the activity of hen egg-white lysozymeProceedings of the Royal Society of London. B. Biological Sciences, 1967