Measurement of relaxation time constants for methyl groups by proton-detected heteronuclear NMR spectroscopy
- 1 October 1991
- journal article
- Published by Elsevier in Chemical Physics Letters
- Vol. 185 (1-2) , 41-46
- https://doi.org/10.1016/0009-2614(91)80136-l
Abstract
No abstract availableKeywords
This publication has 19 references indexed in Scilit:
- Intramolecular motions of a zinc finger DNA-binding domain from Xfin characterized by proton-detected natural abundance carbon-13 heteronuclear NMR spectroscopyJournal of the American Chemical Society, 1991
- Analysis of the backbone dynamics of interleukin-1.beta. using two-dimensional inverse detected heteronuclear nitrogen-15-proton NMR spectroscopyBiochemistry, 1990
- Backbone dynamics of proteins as studied by nitrogen-15 inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nucleaseBiochemistry, 1989
- [18] Interpreting protein dynamics with nuclear magnetic resonance relaxation measurementsPublished by Elsevier ,1989
- Measurement of 13C relaxation times in proteins by two-dimensional heteronuclear 1H-13C correlation spectroscopyJournal of the American Chemical Society, 1988
- The observation of chain motion in macromolecules by carbon-13 and deuterium nuclear magnetic resonance spectroscopyThe Journal of Physical Chemistry, 1985
- Nuclear magnetic resonance studies on bacterial dihydrofolate reductase containing [methyl-13C]methionineBiochemistry, 1978
- Applications of natural-abundance nitrogen-15 nuclear magnetic resonance to large biochemically important molecules.Proceedings of the National Academy of Sciences, 1975
- Theory and practice for studies of peptides by 15N nuclear magnetic resonance at natural abundance: gramicidin SNature, 1975
- Conformation and segmental motion of native and denatured ribonuclease A in solution. Application of natural-abundance carbon-13 partially relaxed Fourier transform nuclear magnetic resonanceJournal of the American Chemical Society, 1971