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本文用具有各向异性的光学晶体模拟肌肉收缩蛋白质分子，给出了描述收缩蛋白质光学特性的极化率张量表示，并讨论了在蛋白质分子运动过程中极化率张量的变化规律。基于这一理论分析，根据用光的椭圆偏振技术测得的单根青蛙肌纤维在僵直状态和松弛状态及在不同温度下的实验结果，我们认为，当肌纤维处于僵直状态时，其内部肌球蛋白分子（横桥部分）与肌动蛋白分子空间距离近，相互作用力强；而在松弛状态时，两种收缩蛋白分子空间距离远，相互作用力弱；当改变肌纤维所处溶液温度时，横桥与肌动蛋白分子的相对空间取向和相互作用力受到影响，较高温度时分子热运动会削弱肌球蛋白分子和肌动蛋白分子之间的作用，使横桥向粗肌丝骨架靠拢．
In this paper, anisotropic optical crystals are used to simulate muscle contractile protein molecules. A polarizability tensor representation describing the optical properties of the contractile proteins is given. The variation of the polarizability tensor in the process of protein molecular motion is discussed. Based on this theoretical analysis, based on the experimental results of the rigid frog muscle fiber in the rigid and relaxed frogs measured by the light elliptical polarization technique and at different temperatures, we think that when the muscle fiber is in a stiff state, its internal myosin The molecular (cross-bridge part) and actin molecules are close to each other in spatial distance and strong in interaction. In the relaxed state, the two contractile proteins are far away from each other in space and have weak interaction force. When the temperature of the solution in the muscle fiber is changed, The relative spatial orientation and interaction force between the bridge and the actin molecules are affected. At higher temperatures, the molecular heat movement will weaken the interaction between myosin molecules and actin molecules and bring the transverse bridge to the thick myofilament.