Solution NMR Measurement of Amide Proton Chemical Shift Anisotropy in 15N-Enriched Proteins. Correlation with Hydrogen Bond Length-Reference-Cited by-同舟云学术

Solution NMR Measurement of Amide Proton Chemical Shift Anisotropy in 15N-Enriched Proteins. Correlation with Hydrogen Bond Length

Published:1997-08-01 Issue:34 Volume:119 Page:8076-8082
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Tjandra Nico¹,Bax Ad¹

Affiliation:

1. Contribution from the Laboratory of Biophysical Chemistry, National Heart, Lung, and Blood Institute, and Laboratory of Chemical Physics, National Institute 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/ja970876e

Reference57 articles.

1. Isotactic polymerization of C-3-branched .alpha.-olefins: conformation of the monomer

2. Conformation-dependent13C chemical shifts: A new means of conformational characterization as obtained by high-resolution solid-state13C NMR

3. Secondary and Tertiary Structural Effects on Protein NMR Chemical Shifts: an ab Initio Approach

4. Chemical shifts and three-dimensional protein structures

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