Increasing the Accuracy of Solution NMR Structures of Membrane Proteins by Application of Residual Dipolar Couplings. High-Resolution Structure of Outer Membrane Protein A-Reference-Cited by-同舟云学术

Increasing the Accuracy of Solution NMR Structures of Membrane Proteins by Application of Residual Dipolar Couplings. High-Resolution Structure of Outer Membrane Protein A

Published:2006-05-01 Issue:21 Volume:128 Page:6947-6951
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Cierpicki Tomasz¹,Liang Binyong¹,Tamm Lukas K.¹,Bushweller John H.¹

Affiliation:

1. Contribution from the Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia 22908, and Department of Chemistry, University of Virginia, Charlottesville, Virginia 22906

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja0608343

Reference34 articles.

1. Solution Structure of the Transmembrane H+-Transporting Subunit c of the F1Fo ATP Synthase

2. NMR Structure Determination of a Membrane Protein with Two Transmembrane Helices in Micelles: MerF of the Bacterial Mercury Detoxification System,

3. NMR Assignments for a Helical 40 kDa Membrane Protein

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