Determination of solution structures of proteins up to 40 kDa using CS-Rosetta with sparse NMR data from deuterated samples
Author:
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Reference45 articles.
1. Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
2. High-Resolution Nuclear Magnetic Resonance Spectra of Selectively Deuterated Staphylococcal Nuclease
3. Direct Measurement of Distances and Angles in Biomolecules by NMR in a Dilute Liquid Crystalline Medium
4. Global folds of proteins with low densities of NOEs using residual dipolar couplings: application to the 370-residue maltodextrin-binding protein
5. Solution Structure of the 128 kDa Enzyme I Dimer from Escherichia coli and Its 146 kDa Complex with HPr Using Residual Dipolar Couplings and Small- and Wide-Angle X-ray Scattering
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