Completely Automated, Highly Error-Tolerant Macromolecular Structure Determination from Multidimensional Nuclear Overhauser Enhancement Spectra and Chemical Shift Assignments-Reference-Cited by-同舟云学术

Completely Automated, Highly Error-Tolerant Macromolecular Structure Determination from Multidimensional Nuclear Overhauser Enhancement Spectra and Chemical Shift Assignments

Published:2004-04-30 Issue:20 Volume:126 Page:6258-6273
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Kuszewski John¹,Schwieters Charles D.¹,Garrett Daniel S.¹,Byrd R. Andrew¹,Tjandra Nico¹,Clore G. Marius¹

Affiliation:

1. Contribution from the Division of Computational Bioscience, Building 12A, Center for Information Technology, National Institutes of Health, Bethesda, Maryland 20892-5624, Laboratory of Chemical Physics, Building 5, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, Structural Biophysics Laboratory, National Cancer Institute, P.O. Box B, Frederick, Maryland 21702-1201, and Laboratory of Biophysical Chemistry, Building 50,...

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja049786h

Reference58 articles.

1. Direct Measurement of Distances and Angles in Biomolecules by NMR in a Dilute Liquid Crystalline Medium

2. Rapid determination of protein folds using residual dipolar couplings

3. Protein Structure Determination Using Molecular Fragment Replacement and NMR Dipolar Couplings

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