Contact Model for the Prediction of NMR N−H Order Parameters in Globular Proteins
- 1 October 2002
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 124 (43) , 12654-12655
- https://doi.org/10.1021/ja027847a
Abstract
An analytical relationship is presented for the estimation of NMR S2 order parameters of N−HN vectors of the protein backbone from high-resolution protein structures. The relationship solely depends on close contacts of the peptide plane to the rest of the protein. Application of the relationship to a number of proteins with high-resolution X-ray and NMR structures yields S2 values that are in good agreement with the ones determined from experimental relaxation data.Keywords
This publication has 22 references indexed in Scilit:
- A refined solution structure of hen lysozyme determined using residual dipolar coupling dataProtein Science, 2001
- Thermodynamic Interpretation of NMR Relaxation Parameters in Proteins in the Presence of Motional CorrelationsThe Journal of Physical Chemistry B, 2000
- Characterization of Collective and Anisotropic Reorientational Protein DynamicsPhysical Review Letters, 2000
- Relationships between protein structure and dynamics from a database of NMR-derived backbone order parametersJournal of Molecular Biology, 2000
- New techniques in structural NMR — anisotropic interactionsNature Structural & Molecular Biology, 1998
- Validation of Protein Structure from Anisotropic Carbonyl Chemical Shifts in a Dilute Liquid Crystalline PhaseJournal of the American Chemical Society, 1998
- Three‐dimensional solution structure of the HIV‐1 protease complexed with DMP323, a novel cyclic urea‐type inhibitor, determined by nuclear magnetic resonance spectroscopyProtein Science, 1996
- Human Interleukin-4 and Variant R88Q: Phasing X-ray Diffraction Data by Molecular Replacement Using X-ray and Nuclear Magnetic Resonance ModelsJournal of Molecular Biology, 1995
- Loop mobility in a four-helix-bundle protein: nitrogen-15 NMR relaxation measurements on human interleukin-4Biochemistry, 1992
- Structure of ubiquitin refined at 1.8 Å resolutionJournal of Molecular Biology, 1987