Conformations of cysteine disulfides of peptide toxins: Advantage of differentiating forward and reverse asymmetric disulfide conformers
Author:
Affiliation:
1. Department of Chemistry, School of Chemical Sciences, Central University of Karnataka, Kalaburagi, Karnataka, India
Funder
DST-INSPIRE
Publisher
Informa UK Limited
Subject
Molecular Biology,General Medicine,Structural Biology
Link
https://www.tandfonline.com/doi/pdf/10.1080/07391102.2018.1475257
Reference38 articles.
1. Bibrotoxin, a novel member of the endothelin/sarafotoxin peptide family, from the venom of the burrowing aspAtractaspis bibroni
2. Crystal structure of a Cbtx–AChBP complex reveals essential interactions between snake α-neurotoxins and nicotinic receptors
3. Complex cocktails: the evolutionary novelty of venoms
4. Crystal structure of nicotinic acetylcholine receptor homolog AChBP in complex with an α-conotoxin PnIA variant
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