title: Conformational preferences of sequential fragments of the hinge region of human IgA1 immunoglobulin molecule: II.
abstract: The mean solution conformation of tetrapeptide fragments of the hinge region of human IgA1 molecule was investigated by CD and 13C-NMR methods. Distinct conformational differences for the partial sequences were found. Tetrapeptides with the Thr-Pro-Ser-Pro sequence were found to show a clear preference for the beta-turn conformation. Conformational equilibria of these peptides are only slightly affected by acetylation or pH changes. In the case of Pro-Thr-Pro-Ser tetrapeptides conformational equilibria are dominated by unordered forms.
authors.affiliation: University Hospital, Boston University, MA 02118.
authors.forename: J
authors.initials: J
authors.lastname: Burton
authors.forename: S G
authors.initials: SG
authors.lastname: Wood
authors.forename: A
authors.initials: A
authors.lastname: Pedyczak
authors.forename: I Z
authors.initials: IZ
authors.lastname: Siemion
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D006801:Humans; D007070:Immunoglobulin A / Q000145:classification; D007128:Immunoglobulin Fragments; D008969:Molecular Sequence Data; D009842:Oligopeptides; D011487:Protein Conformation
chemical_list: D007070:Immunoglobulin A; D007128:Immunoglobulin Fragments; D009842:Oligopeptides