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Cited by 227

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

New methods of structure refinement for macromolecular structure determination by NMR

Open access
Clore, G. Marius, Gronenborn, Angela M.·1998·Proceedings of the National Academy of Sciences

Abstract

Recent advances in multidimensional NMR methodology have permitted solution structures of proteins in excess of 250 residues to be solved. In this paper, we discuss several methods of structure refinement that promise to increase the accuracy of macromolecular structures determined by NMR. These methods include the use of a conformational database potential and direct refinement against three-bond coupling constants, secondary 13 C shifts, 1 H shifts, T 1 /T 2 ratios, and residual dipolar couplings. The latter two measurements provide long range restraints that are not accessible by other solution NMR parameters.

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Crossref · 10.1073/pnas.95.11.5891

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Metadata

Authors
Clore, G. M., & Gronenborn, A. M.
Venue
Proceedings of the National Academy of Sciences
Published
1998-05-26
Volume
95
Issue
11
Pages
5891-5898
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2156995522
Cited by
227
References
1
FWCI
13.31
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: New methods of structure refinement for macromolecular structure determination by NMR. https://app.cochat.ai/papers/10.1073/pnas.95.11.5891
The paper
Clore, G. M., & Gronenborn, A. M. (1998). New methods of structure refinement for macromolecular structure determination by NMR. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.95.11.5891

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.