Efficient determination of the most favoured orientations of protein domains from paramagnetic NMR data
From MaRDI portal
Publication:5486442
Recommendations
- Reconstruction of orientations of a moving protein domain from paramagnetic data
- Conformational freedom of proteins and the maximal probability of sets of orientations
- Joining RDC data from flexible protein domains
- Protein Structure Prediction Using Residual Dipolar Couplings
- Looking for central tendencies in the conformational freedom of proteins using NMR measurements
Cited in
(11)- Joining RDC data from flexible protein domains
- Reconstruction of orientations of a moving protein domain from paramagnetic data
- Convex hulls of orbits and orientations of a moving protein domain
- Inferential structure determination from NMR data
- Restoring orientational distribution function of particles
- Protein Structure Prediction Using Residual Dipolar Couplings
- Model-Based Assignment and Inference of Protein Backbone Nuclear Magnetic Resonances
- Extended Abstract: Structure Determination of Symmetric Protein Complexes by a Complete Search of Symmetry Configuration Space Using NMR Distance Restraints
- Looking for central tendencies in the conformational freedom of proteins using NMR measurements
- Conformational freedom of proteins and the maximal probability of sets of orientations
- Uniqueness and degeneracy in the localization of rigid structural elements in paramagnetic proteins
This page was built for publication: Efficient determination of the most favoured orientations of protein domains from paramagnetic NMR data
Report a bug (only for logged in users!)Click here to report a bug for this page (MaRDI item Q5486442)