Multiple Alignment of Membrane Proteins for Measuring Residual Dipolar Couplings Using Lanthanide Ions Bound to a Small Metal Chelator
Author:
Affiliation:
1. Biochemistry Department, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja067089e
Reference22 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. Direct Measurement of Distances and Angles in Biomolecules by NMR in a Dilute Liquid Crystalline Medium
3. Residual Dipolar Couplings in NMR Structure Analysis
4. Residual Dipolar Couplings in Structure Determination of Biomolecules
5. NMR Structure Determination of a Membrane Protein with Two Transmembrane Helices in Micelles: MerF of the Bacterial Mercury Detoxification System,
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