Dynamical Mapping of E. coli Thioredoxin via 13C NMR Relaxation Analysis
- 1 January 1996
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 118 (39), 9255-9264
- https://doi.org/10.1021/ja960877r
Abstract
No abstract availableKeywords
This publication has 43 references indexed in Scilit:
- Protein Backbone Dynamics Revealed by Quasi Spectral Density Function Analysis of Amide N-15 NucleiBiochemistry, 1995
- Comparison of the Backbone Dynamics of a Folded and an Unfolded SH3 Domain Existing in Equilibrium in Aqueous BufferBiochemistry, 1995
- Proton-detected NMR relaxation of methylene carbons via stereoselective and random fractional deuterationJournal of the American Chemical Society, 1993
- Dynamics of methyl groups in proteins as studied by proton-detected carbon-13 NMR spectroscopy. Application to the leucine residues of staphylococcal nucleaseBiochemistry, 1992
- 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
- Crystal structure of thioredoxin from Escherichia coli at 1.68 Å resolutionJournal of Molecular Biology, 1990
- Regulation of NADP‐malate dehydrogenase by the light‐actuated ferredoxin/thioredoxin system of chloroplastsFEBS Letters, 1977
- A 13C spin‐lattice relaxation study of dipeptides containing glycine and proline: Mobility of the cyclic proline side chainBiopolymers, 1975
- Amber Mutants of the -Ketoglutarate Dehydrogenase Gene of Escherichia coli K12Journal of General Microbiology, 1972
- Effect of CH scalar coupling on carbon-13 transverse relaxation timesJournal of the American Chemical Society, 1971