Literature DB >> 21488042

Overview on the use of NMR to examine protein structure.

Vincent Breukels1, Albert Konijnenberg, Sanne M Nabuurs, Jurgen F Doreleijers, Nadezda V Kovalevskaya, Geerten W Vuister.   

Abstract

Any protein structure determination process contains several steps, starting from obtaining a suitable sample, then moving on to acquiring data and spectral assignment, and lastly to the final steps of structure determination and validation. This unit describes all of these steps, starting with the basic physical principles behind NMR and some of the most commonly measured and observed phenomena such as chemical shift, scalar and residual coupling, and the nuclear Overhauser effect. Then, in somewhat more detail, the process of spectral assignment and structure elucidation is explained. Furthermore, the use of NMR to study protein-ligand interaction, protein dynamics, or protein folding is described.
© 2011 by John Wiley & Sons, Inc.

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Year:  2011        PMID: 21488042     DOI: 10.1002/0471140864.ps1705s64

Source DB:  PubMed          Journal:  Curr Protoc Protein Sci        ISSN: 1934-3655


  2 in total

1.  The structure of Vibrio cholerae FeoC reveals conservation of the helix-turn-helix motif but not the cluster-binding domain.

Authors:  Janae B Brown; Mark A Lee; Aaron T Smith
Journal:  J Biol Inorg Chem       Date:  2022-07-07       Impact factor: 3.862

2.  Simple high-resolution NMR spectroscopy as a tool in molecular biology.

Authors:  Luca Mureddu; Geerten W Vuister
Journal:  FEBS J       Date:  2019-02-14       Impact factor: 5.542

  2 in total

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