我们在20 - 100 ^{ \circ } $C for a collagen fibril taken from rat's tendon. The hydration change under heating and the damping decrement were measured as well. At physiological temperatures $ 25-45^{ \circ} $C Young's modulus decreases, which can be interpreted as instability of collagen. For temperatures between $ 45-80^{ \circ} $C Young's modulus first stabilizes and then increases with decreasing the temperature. The hydrated water content and the damping decrement have strong maxima in the interval $ 70-80^{\circ} $C indicating on complex inter-molecular structural changes in the fibril. All these effects disappear after heat-denaturating the sample at $ 120^ \circ $C的温度范围内测量杨氏模量。我们的主要结果是一个五阶段的机制，其中一个单一的胶原蛋白在生理温度下的不稳定性是补偿的胶原蛋白分子之间的相互作用在原纤维。
英文摘要：
We measured Young's modulus at temperatures ranging from 20 to 100 ^{\circ}$C for a collagen fibril taken from rat's tendon. The hydration change under heating and the damping decrement were measured as well. At physiological temperatures $25-45^{\circ}$C Young's modulus decreases, which can be interpreted as instability of collagen. For temperatures between $45-80^{\circ}$C Young's modulus first stabilizes and then increases with decreasing the temperature. The hydrated water content and the damping decrement have strong maxima in the interval $70-80^{\circ}$C indicating on complex inter-molecular structural changes in the fibril. All these effects disappear after heat-denaturating the sample at $120^\circ$C. Our main result is a five-stage mechanism by which the instability of a single collagen at physiological temperatures is compensated by the interaction between collagen molecules within the fibril.
