Determination of the nuclear magnetic resonance solution structure of the DNA-binding domain (residues 1 to 69) of the 434 repressor and comparison with the X-ray crystal structure
- 5 February 1992
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 223 (3), 743-767
- https://doi.org/10.1016/0022-2836(92)90987-u
Abstract
No abstract availableKeywords
This publication has 49 references indexed in Scilit:
- Precise vicinal coupling constants3JHNα in proteins from nonlinear fits of J-modulated [15N,1H]-COSY experimentsJournal of Biomolecular NMR, 1992
- Efficient analysis of protein 2D NMR spectra using the software packageEASYJournal of Biomolecular NMR, 1991
- Studies of slow conformational equilibria in macromolecules by exchange of heteronuclear longitudinal 2-spin-order in a 2D difference correlation experimentJournal of Biomolecular NMR, 1991
- The phage 434 complex at 2.5 Å resolutionJournal of Molecular Biology, 1991
- Comparison of the high-resolution structures of the α-amylase inhibitor tendamistat determined by nuclear magnetic resonance in solution and by X-ray diffraction in single crystalsJournal of Molecular Biology, 1989
- Structure of the amino-terminal domain of phage 434 represser at 2.0 Å resolutionJournal of Molecular Biology, 1989
- Structure of phage 434 cro protein at 2.35 Å resolutionJournal of Molecular Biology, 1989
- Improved spectral resolution in COSY 1H NMR spectra of proteins via double quantum filteringBiochemical and Biophysical Research Communications, 1983
- Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonanceJournal of Molecular Biology, 1983
- A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromoleculesBiochemical and Biophysical Research Communications, 1980