13C−13C Rotational Resonance Width Distance Measurements in Uniformly 13C-Labeled Peptides-Reference-Cited by-同舟云学术

13C−13C Rotational Resonance Width Distance Measurements in Uniformly 13C-Labeled Peptides

Published:2003-11-21 Issue:50 Volume:125 Page:15623-15629
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Ramachandran Ramesh¹,Ladizhansky Vladimir¹,Bajaj Vikram S.¹,Griffin Robert G.¹

Affiliation:

1. Contribution from the Francis Bitter Magnet Laboratory and Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139-4307

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja037761x

Reference60 articles.

1. Rotational resonance determination of the structure of an enzyme-inhibitor complex: phosphorylation of an (aminoalkyl)phosphinate inhibitor of D-alanyl-D-alanine ligase by ATP

2. Determination of Membrane Protein Structure by Rotational Resonance NMR: Bacteriorhodopsin

3. Determination of internuclear distances and the orientation of functional groups by solid-state NMR: Rotational resonance study of the conformation of retinal in bacteriorhodopsin

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