NMR Assignments for a Helical 40 kDa Membrane Protein-Reference-Cited by-同舟云学术

NMR Assignments for a Helical 40 kDa Membrane Protein

Published:2004-03-31 Issue:16 Volume:126 Page:5048-5049
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Oxenoid Kirill¹,Kim Hak Jun¹,Jacob Jaison¹,Sönnichsen Frank D.¹,Sanders Charles R.¹

Affiliation:

1. Department of Biochemistry and Center for Structural Biology, Vanderbilt University, Nashville, Tennessee 37232-8725, and Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, Ohio 44106-4970

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja049916m

Reference27 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. TROSY in NMR studies of the structure and function of large biological macromolecules

3. NMR solution structure determination of membrane proteins reconstituted in detergent micelles

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