Variation of Molecular Alignment as a Means of Resolving Orientational Ambiguities in Protein Structures from Dipolar Couplings
- 30 April 2000
- journal article
- editorial
- Published by Elsevier in Journal of Magnetic Resonance
- Vol. 143 (2), 402-406
- https://doi.org/10.1006/jmre.2000.2049
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- Residual dipolar coupling derived orientational constraints on ligand geometry in a 53 kDa protein-ligand complexJournal of Molecular Biology, 1999
- Impact of Residual Dipolar Couplings on the Accuracy of NMR Structures Determined from a Minimal Number of NOE RestraintsJournal of the American Chemical Society, 1999
- Domain Orientation and Dynamics in Multidomain Proteins from Residual Dipolar CouplingsBiochemistry, 1999
- NMR assignments, secondary structure, and global fold of calerythrin, an EF‐hand calcium‐binding protein from Saccharopolyspora erythraeaProtein Science, 1999
- Recognition of protein folds via dipolar couplingsJournal of Biomolecular NMR, 1999
- Modulation of the Alignment Tensor of Macromolecules Dissolved in a Dilute Liquid Crystalline MediumJournal of the American Chemical Society, 1998
- New techniques in structural NMR — anisotropic interactionsNature Structural & Molecular Biology, 1998
- Direct Measurement of Distances and Angles in Biomolecules by NMR in a Dilute Liquid Crystalline MediumScience, 1997
- Nuclear magnetic dipole interactions in field-oriented proteins: information for structure determination in solution.Proceedings of the National Academy of Sciences, 1995
- High-Resolution NMR of Liquids and Gases: Effects of Magnetic-Field-Induced Molecular AlignmentPublished by Elsevier ,1987