Determination of protein global folds using backbone residual dipolar coupling and long-range NOE restraints.
- 1 January 2003
- journal article
- Published by Springer Nature in Journal of Biomolecular NMR
- Vol. 25 (1), 63-71
- https://doi.org/10.1023/a:1021954812977
Abstract
No abstract availableKeywords
This publication has 33 references indexed in Scilit:
- De novo determination of protein structure by NMR using orientational and long-range order restraintsJournal of Molecular Biology, 2000
- Variation of Molecular Alignment as a Means of Resolving Orientational Ambiguities in Protein Structures from Dipolar CouplingsJournal of Magnetic Resonance, 2000
- A method for incorporating dipolar couplings into structure calculations in cases of (near) axial symmetry of alignment.Journal of Biomolecular NMR, 2000
- Order Matrix Analysis of Residual Dipolar Couplings Using Singular Value DecompositionJournal of Magnetic Resonance, 1999
- Bicelle-based liquid crystals for NMR-measurement of dipolar couplings at acidic and basic pH valuesJournal of Biomolecular NMR, 1999
- Residual dipolar couplings as new conformational restraints in isotopically 13C‐enriched oligosaccharidesFEBS Letters, 1998
- Some NMR Experiments and a Structure Determination Employing a {15N,2H} Enriched ProteinJournal of Biomolecular NMR, 1998
- NMR evidence for slow collective motions in cyanometmyoglobinNature Structural & Molecular Biology, 1997
- High-resolution heteronuclear NMR of human ubiquitin in an aqueous liquid crystalline medium.Journal of Biomolecular NMR, 1997
- Protein φ and ψ dihedral restraints determined from multidimensional hypersurface correlations of backbone chemical shifts and their use in the determination of protein tertiary structuresJournal of Biomolecular NMR, 1997