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Deuterium labelling in NMR structural analysis of larger proteins

Published online by Cambridge University Press:  17 March 2009

David M. LeMaster
David M. LeMaster
Affiliation:
Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208, USA
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Extract

In the last few years since the early NMR structural studies of small proteins such as glucagon (Braun et al. 1983) and lac represser headpiece (Zuiderweg et al. 1984) the quality of the structure determinations have improved considerably. Of major importance has been the introduction of phase sensitive detection in the Tl dimension (States et al. 1982; Marion & Wüthrich, 1983) which has allowed for absorption presentation of 2D data with the resulting enhancement in resolution, accuracy of coupling constant measurements and accuracy of peak volume integrations. Introduction of new pulse sequences, advances in instrumentation and further developments in the structure calculation algorithms have also helped improve the quality of NMR structural analyses of proteins.

Type
Research Article
Information
Quarterly Reviews of Biophysics , Volume 23 , Issue 2 , May 1990 , pp. 133 - 174
Copyright
Copyright © Cambridge University Press 1990

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