胶原蛋白的松弛行为
Relaxation behavior of collagen.
作者信息
Stefanou H, Woodward A E, Morrow D
出版信息
Biophys J. 1973 Aug;13(8):772-9. doi: 10.1016/S0006-3495(73)86023-0.
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.
使用扭摆研究了牛肌腱纯化胶原蛋白在120开尔文至360开尔文温度范围内、0.3至1赫兹频率下的动态力学性能。在所研究的温度范围内，观察到两个损耗峰：一个在约200开尔文处的β峰，以及在约280开尔文处大约大五倍的α峰。α转变温度显示取决于含水量，随水量增加而降低并向低温移动。还对类似样品获得了宽线质子磁共振结果。在约250摄氏度处出现一条窄核磁共振（NMR）线。还研究了收缩形成明胶和交联对胶原蛋白松弛行为的影响。讨论了胶原蛋白在120开尔文至360开尔文范围内发生的运动。
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