title: Conformational change from rigid rod to star: a triple-helical peptide with a linker domain at the C-terminal end.
abstract: Small-angle X-ray scattering and circular dichroism measurements were made for a triple-helical peptide of which one end was linked by the thermally stable trimerization domain of type XIX collagen. The radius of gyration decreased steeply around the transition temperature while the scattering intensity at zero angle did not significantly change, indicating no molar mass change through the conformational transition. Thus, the data were analyzed in terms of the rigid cylinder model for the data at low temperatures and the wormlike star model at high temperatures. It was confirmed that the peptide molecules behave as a rod-like cylinder at low temperature and a semi flexible three-arm star-like chain at high temperature of which the single-coil peptide chain is appreciably extended by the high segment density nearby the linking domain.
authors: Department of Macromolecular Science, Osaka University , 1-1, Machikaneyama-cho, Toyonaka, Osaka 560-0043, Japan.
authors: Ken
authors: K
authors: Terao
authors: Kazunori
authors: K
authors: Mizuno
authors: Hans Peter
authors: HP
authors: Bächinger
mesh_terms: D000595:Amino Acid Sequence; D003094:Collagen / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012399:Rotation; D013696:Temperature
chemical_list: D010446:Peptide Fragments; D003094:Collagen