title: Elastic properties and beta-sheet structure of connectin threads.
abstract: Connectin is a very long and flexible protein of striated muscle, linking myosin filaments to z discs in a sarcomere. Isolated native connectin in solution frequently forms elastic threads upon concentration of the solution, by side-by-side association of molecules. An X-ray diffraction study was performed to examine the presence of beta-sheet structure in artificially prepared threads. The elastic properties of such threads were measured at various temperatures. Negative temperature dependence of the elastic coefficient suggests that the elasticity of connectin threads is due to deformation of the three-dimensional structure and not to rubber-like behavior.
authors.affiliation: Faculty of Pharmaceutical Science, University of Tokyo.
authors.forename: Y
authors.initials: Y
authors.lastname: Mitsui
authors.forename: H
authors.initials: H
authors.lastname: Higuchi
authors.forename: S
authors.initials: S
authors.lastname: Terashima
authors.forename: S
authors.initials: S
authors.lastname: Takahashi
authors.forename: D H
authors.initials: DH
authors.lastname: Hu
authors.forename: K
authors.initials: K
authors.lastname: Maruyama
authors.forename: H
authors.initials: H
authors.lastname: Noda
mesh_terms: D000818:Animals; D002645:Chickens; D064211:Connectin; D004548:Elasticity; D009124:Muscle Proteins; D009132:Muscles / Q000032:analysis*; D011487:Protein Conformation; D011494:Protein Kinases; D013696:Temperature; D014961:X-Ray Diffraction
chemical_list: D064211:Connectin; D009124:Muscle Proteins; D011494:Protein Kinases