Relaxation behavior of collagen.
The dynamic mechanical properties of purified collagen from bovine tendon were studied using a torsion pendulum in the temperature range of 120 degrees -360 degrees K at 0.3-1 cps. In the temperature range studied, two loss peaks were observed: a beta-peak at about 200 degrees K, and an alpha-peak approximately five times larger at about 280 degrees K. The temperature of the alpha-transition is shown to be dependent on water content, decreasing with increasing amount of water and shifting to lower temperatures. Broad-line proton magnetic resonance results were also obtained on similar samples. A narrow nuclear magnetic resonance (NMR) line appears at about 250 degrees C. The effects of shrinkage to form gelatin and of cross-linking on the relaxation behavior of collagen were also studied. The motions taking place in collagen over the 120 degrees -360 degrees K range are discussed.
D000818:Animals; D002417:Cattle; D003094:Collagen; D004548:Elasticity; D005557:Formaldehyde; D005780:Gelatin / Q000032:analysis; D006358:Hot Temperature; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D011489:Protein Denaturation; D013696:Temperature; D013710:Tendons; D014867:Water; D014961:X-Ray Diffraction
D014867:Water; D005557:Formaldehyde; D005780:Gelatin; D003094:Collagen