A new molecular model for collagen elasticity based on synchrotron X-ray scattering evidence.
Collagen is the most abundant structural protein in vertebrates. The specific shape of its stress-strain curve is crucial for the function of a number of organs. Although the macroscopic mechanical behavior of collagen is well known, there is still no explanation of the elastic process at the supramolecular level. We have performed in situ synchrotron x-ray scattering experiments, which show that the amount of lateral molecular order increases upon stretching of collagen fibers. In strain cycling experiments the relation between strain and diffuse equatorial scattering was found to be linear in the "heel" region of the stress-strain curve. A new molecular model for collagen elasticity is proposed, which, based on the existence of thermally activated molecular kinks, reproduces this linearity and gives a simple explanation for the form of the stress-strain curve of collagen.
Misof
K
K
Institut für Materialphysik, Universität Wien, Austria.
Rapp
G
G
Fratzl
P
P
D000818:Animals; D003094:Collagen / Q000737:chemistry* / Q000648:ultrastructure; D004548:Elasticity; D007700:Kinetics; D008956:Models, Chemical; D012044:Regression Analysis; D013314:Stress, Mechanical; D017356:Synchrotrons; D013997:Time Factors; D014714:Vertebrates; D014961:X-Ray Diffraction / Q000295:instrumentation / Q000379:methods
D003094:Collagen