NMR methods for determining disulfide-bond connectivities

Mobli, Mehdi and King, Glenn F. (2010) NMR methods for determining disulfide-bond connectivities. Toxicon, 56 6: 849-854. doi:10.1016/j.toxicon.2010.06.018

Author Mobli, Mehdi
King, Glenn F.
Title NMR methods for determining disulfide-bond connectivities
Journal name Toxicon   Check publisher's open access policy
ISSN 0041-0101; 879-3150
Publication date 2010-11
Sub-type Critical review of research, literature review, critical commentary
DOI 10.1016/j.toxicon.2010.06.018
Volume 56
Issue 6
Start page 849
End page 854
Total pages 6
Place of publication Kidlington, United Kingdom
Publisher Pergamon
Collection year 2011
Language eng
Subject C1
Formatted abstract
Animal toxins are the major class of secreted disulfide-rich proteins, with ~70% containing two or more disulfide bonds. Incorrect pairing of these disulfide bonds typically leads to a non-native three-dimensional fold accompanied by a loss of protein function. Determination of the native disulfide-bond framework is therefore a key component in the structural characterization of toxins. In this article, we review NMR approaches for elucidation of disulfide-bond connectivities. A major advantage of these NMR approaches is that they are non-invasive, leaving the sample intact at the end of the analysis for use in other studies.
Crown Copyright © 2010 Published by Elsevier Ltd.

Keyword Disulfide bond
Disulfide bridge
Cystine Knot
Insecticidal Neurotoxins
Chemical shifts
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes Available online 5 July 2010.

Document type: Journal Article
Sub-type: Critical review of research, literature review, critical commentary
Collections: Official 2011 Collection
Institute for Molecular Bioscience - Publications
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Citation counts: TR Web of Science Citation Count  Cited 22 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 22 times in Scopus Article | Citations
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Created: Sun, 17 Oct 2010, 00:00:43 EST