Determination of the Relative Orientation of the Two Halves of the Domain-Swapped Dimer of Cyanovirin-N in Solution Using Dipolar Couplings and Rigid Body Minimization
- 1 June 2000
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 122 (25) , 6009-6016
- https://doi.org/10.1021/ja000858o
Abstract
No abstract availableKeywords
This publication has 9 references indexed in Scilit:
- Prediction of Sterically Induced Alignment in a Dilute Liquid Crystalline Phase: Aid to Protein Structure Determination by NMRJournal of the American Chemical Society, 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
- Order Matrix Analysis of Residual Dipolar Couplings Using Singular Value DecompositionJournal of Magnetic Resonance, 1999
- Crystal structure of cyanovirin-N, a potent HIV-inactivating protein, shows unexpected domain swappingJournal of Molecular Biology, 1999
- Improving the Packing and Accuracy of NMR Structures with a Pseudopotential for the Radius of GyrationJournal of the American Chemical Society, 1999
- Solution structure of cyanovirin-N, a potent HIV-inactivating proteinNature Structural & Molecular Biology, 1998
- New techniques in structural NMR — anisotropic interactionsNature Structural & Molecular Biology, 1998
- Measurement ofJand Dipolar Couplings from Simplified Two-Dimensional NMR SpectraJournal of Magnetic Resonance, 1998
- Direct Measurement of Distances and Angles in Biomolecules by NMR in a Dilute Liquid Crystalline MediumScience, 1997