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Biochim Biophys Acta Proteins Proteom. 2017 Nov;1865(11 Pt B):1564-1576. doi: 10.1016/j.bbapap.2017.07.005. Epub 2017 Jul 15.

Unraveling the meaning of chemical shifts in protein NMR.

Author information

1
Department of Computing Science, University of Alberta, Edmonton T6G 2E9, Canada; Department of Biological Sciences, University of Alberta, Edmonton T6G 2E8, Canada.
2
Department of Computing Science, University of Alberta, Edmonton T6G 2E9, Canada; Department of Biological Sciences, University of Alberta, Edmonton T6G 2E8, Canada. Electronic address: david.wishart@ualberta.ca.

Abstract

Chemical shifts are among the most informative parameters in protein NMR. They provide wealth of information about protein secondary and tertiary structure, protein flexibility, and protein-ligand binding. In this report, we review the progress in interpreting and utilizing protein chemical shifts that has occurred over the past 25years, with a particular focus on the large body of work arising from our group and other Canadian NMR laboratories. More specifically, this review focuses on describing, assessing, and providing some historical context for various chemical shift-based methods to: (1) determine protein secondary and super-secondary structure; (2) derive protein torsion angles; (3) assess protein flexibility; (4) predict residue accessible surface area; (5) refine 3D protein structures; (6) determine 3D protein structures and (7) characterize intrinsically disordered proteins. This review also briefly covers some of the methods that we previously developed to predict chemical shifts from 3D protein structures and/or protein sequence data. It is hoped that this review will help to increase awareness of the considerable utility of NMR chemical shifts in structural biology and facilitate more widespread adoption of chemical-shift based methods by the NMR spectroscopists, structural biologists, protein biophysicists, and biochemists worldwide. This article is part of a Special Issue entitled: Biophysics in Canada, edited by Lewis Kay, John Baenziger, Albert Berghuis and Peter Tieleman.

KEYWORDS:

Chemical shift; NMR; Prediction; Protein; Structure

PMID:
28716441
DOI:
10.1016/j.bbapap.2017.07.005
[Indexed for MEDLINE]

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