title: NMR methods for determining disulfide-bond connectivities.
abstract: Animal toxins are the major class of secreted disulfide-rich proteins, with approximately 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.
authors.affiliation: Institute for Molecular Bioscience, The University of Queensland, St. Lucia QLD 4072, Australia.
authors.forename: Mehdi
authors.initials: M
authors.lastname: Mobli
authors.forename: Glenn F
authors.initials: GF
authors.lastname: King
mesh_terms: D000818:Animals; D055598:Chemical Phenomena; D004220:Disulfides / Q000737:chemistry*; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013438:Sulfhydryl Compounds / Q000737:chemistry; D014118:Toxins, Biological / Q000737:chemistry*
chemical_list: D004220:Disulfides; D013438:Sulfhydryl Compounds; D014118:Toxins, Biological