Journal
TOXICON
Volume 56, Issue 6, Pages 849-854Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.toxicon.2010.06.018
Keywords
Disulfide bond; Disulfide bridge; NMR; Toxin; Protein; Peptide; Selenocysteine
Categories
Funding
- Australian Research Council [DP0774245, DP0878450]
- Australian Research Council [DP0878450, DP0774245] Funding Source: Australian Research Council
Ask authors/readers for more resources
Animal toxins are the major class of secreted disulfide-rich proteins, with similar to 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 (C) 2010 Published by Elsevier Ltd. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available