Enhanced measurement of residual chemical shift anisotropy for small molecule structure elucidation-Reference-Cited by-同舟云学术

Enhanced measurement of residual chemical shift anisotropy for small molecule structure elucidation

Published:2018 Issue:34 Volume:54 Page:4254-4257
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Liu Yizhou¹²³⁴^ORCID,Cohen Ryan D.¹²³⁴^ORCID,Gustafson Kirk R.⁵⁶⁷⁸⁴^ORCID,Martin Gary E.¹²³⁴^ORCID,Williamson R. Thomas¹²³⁴^ORCID

Affiliation:

1. Structure Elucidation Group, Process and Analytical Research and Development

2. Merck & Co. Inc.

3. Rahway

4. USA

5. Molecular Targets Program

6. Center for Cancer Research

7. National Cancer Institute

8. Frederick

Abstract

A simple strategy is introduced to accurately measure residual chemical shift anisotropies (RCSAs) from strong molecular alignment in the mesophase of poly-γ-(benzyl-l-glutamate). The improved data quality greatly enhances the utility of RCSA in small molecule structure analysis.

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2018/CC/C8CC00552D

Reference30 articles.

1. Validation of Protein Structure from Anisotropic Carbonyl Chemical Shifts in a Dilute Liquid Crystalline Phase

2. Measurement of Proton, Nitrogen, and Carbonyl Chemical Shielding Anisotropies in a Protein Dissolved in a Dilute Liquid Crystalline Phase

3. 15N chemical shift anisotropy in protein structure refinement and comparison with NH residual dipolar couplings

4. Carbonyl CSA Restraints from Solution NMR for Protein Structure Refinement

5. A device for the measurement of residual chemical shift anisotropy and residual dipolar coupling in soluble and membrane-associated proteins

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