Four-Dimensional NMR Spectroscopy of a 723-Residue Protein: Chemical Shift Assignments and Secondary Structure of Malate Synthase G
- 1 August 2002
- journal article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 124 (34), 10025-10035
- https://doi.org/10.1021/ja0205636
Abstract
F1000Prime Recommended Article: Four-dimensional NMR spectroscopy of a 723-residue protein: chemical shift assignments and secondary structure of malate synthase g.Keywords
This publication has 45 references indexed in Scilit:
- Ligand-induced structural changes to maltodextrin-binding protein as studied by solution NMR spectroscopyJournal of Molecular Biology, 2001
- Global folds of proteins with low densities of NOEs using residual dipolar couplings: application to the 370-residue maltodextrin-binding proteinJournal of Molecular Biology, 2000
- Crystal Structure of Escherichia coli Malate Synthase G Complexed with Magnesium and Glyoxylate at 2.0 Å Resolution: Mechanistic Implications,,Biochemistry, 2000
- Orienting domains in proteins using dipolar couplings measured by liquid-state NMR: differences in solution and crystal forms of maltodextrin binding protein loaded with β-cyclodextrinJournal of Molecular Biology, 2000
- Transverse Relaxation-Optimized Spectroscopy (TROSY) for NMR Studies of Aromatic Spin Systems in 13C-Labeled ProteinsJournal of the American Chemical Society, 1998
- Characterizing the Use of Perdeuteration in NMR Studies of Large Proteins:13C,15N and1H Assignments of Human Carbonic Anhydrase IIJournal of Molecular Biology, 1996
- Monitoring Macromolecular Motions on Microsecond to Millisecond Time Scales by R1ρ−R1 Constant Relaxation Time NMR SpectroscopyJournal of the American Chemical Society, 1996
- NMRPipe: A multidimensional spectral processing system based on UNIX pipesJournal of Biomolecular NMR, 1995
- Carbon-hydrogen insertions in the reactions of Fischer carbene complexes with ketene acetalsJournal of the American Chemical Society, 1992
- The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopyBiochemistry, 1992