期刊
TOXICON
卷 56, 期 6, 页码 849-854出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.toxicon.2010.06.018
关键词
Disulfide bond; Disulfide bridge; NMR; Toxin; Protein; Peptide; Selenocysteine
资金
- Australian Research Council [DP0774245, DP0878450]
- Australian Research Council [DP0878450, DP0774245] Funding Source: Australian Research Council
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据