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Distance geometry and related methods for protein structure determination from NMR data

Published online by Cambridge University Press:  17 March 2009

Werner Braun
Werner Braun
Affiliation:
Institutfür Molekularbiologie u. Biophysik, Eidgenössische Technische Hochschule, Zürich - Hönggerberg, Cff-8093 Zürich, Switzerland
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Extract

The method of choice to reveal the conformation of protein molecules in atomic detail has been X-ray single-crystal analysis. Since the first structural analysis of diffraction patterns, computer calculations have been an important tool in these studies (Blundell & Johnson, 1976). As is described by Sheldrick (1985), it has been taken for granted that a necessary first step in the determination of a protein structure would be writing computer programs to fit structure factors. In contrast the combined use of the structural analysis of NMR data and computer calculations has been quite limited. An early attempt of such structural calculations was the quantitative determination of mononucleotide conformations in solution using lanthanide ion shifts (Barry et al. 1971).

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Research Article
Information
Quarterly Reviews of Biophysics , Volume 19 , Issue 3-4 , May 1987 , pp. 115 - 157
Copyright
Copyright © Cambridge University Press 1987

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