title: Origin of the positive 225-230 nm circular dichroism band in proteins. Its application to conformational analysis.
abstract: The 225-230 nm circular dichroism band found in many disulfide-containing proteins and peptides is sensitive to environmental changes. This band is assigned to the disulfide bond, the conformation of which influences both the intensity and lambda max of the band. This property can be used to monitor subtle conformation changes observed in many polypeptides. Examples using the alpha-neurotoxins of elapid venoms and neurohypophyseal hormones are discussed.
authors.affiliation: Department of Chemistry, University of Essex, Colchester, U.K.
authors.forename: R C
authors.initials: RC
authors.lastname: Hider
authors.forename: G
authors.initials: G
authors.lastname: Kupryszewski
authors.forename: P
authors.initials: P
authors.lastname: Rekowski
authors.forename: B
authors.initials: B
authors.lastname: Lammek
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D004546:Elapid Venoms; D008958:Models, Molecular; D011487:Protein Conformation; D011506:Proteins; D013056:Spectrophotometry, Ultraviolet / Q000379:methods; D014667:Vasopressins
chemical_list: D004546:Elapid Venoms; D011506:Proteins; D014667:Vasopressins