Using the Experimentally Determined Components of the Overall Rotational Diffusion Tensor To Restrain Molecular Shape and Size in NMR Structure Determination of Globular Proteins and Protein−Protein Complexes-Reference-Cited by-同舟云学术

Using the Experimentally Determined Components of the Overall Rotational Diffusion Tensor To Restrain Molecular Shape and Size in NMR Structure Determination of Globular Proteins and Protein−Protein Complexes

Published:2009-06-18 Issue:27 Volume:131 Page:9522-9531
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Ryabov Yaroslav¹,Suh Jeong-Yong¹,Grishaev Alexander¹,Clore G. Marius¹,Schwieters Charles D.¹

Affiliation:

1. Division of Computational Bioscience, Building 12A, Center for Information Technology, National Institutes of Health, Bethesda, Maryland 20892-5624, and Laboratory of Chemical Physics, Building 5, National Institutes of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja902336c

Reference56 articles.

1. NMR with Proteins and Nucleic Acids

2. Determination of Three-Dimensional Structures of Proteins and Nucleic Acids in Solution by Nuclear Magnetic Resonance Spectroscop

3. New methods of structure refinement for macromolecular structure determination by NMR

4. Dipolar Couplings in Macromolecular Structure Determination

5. NMR structures of biomolecules using field oriented media and residual dipolar couplings

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