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National Academy of Sciences, Proceedings of the National Academy of Sciences, 11(95), p. 5891-5898, 1998

DOI: 10.1073/pnas.95.11.5891

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New methods of structure refinement for macromolecular structure determination by NMR

Journal article published in 1998 by G. Marius Clore, Angela M. Gronenborn ORCID
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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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.