Frank E G, Namiot V A, Esipova N G
Biofizika. 1984 May-Jun;29(3):494-6.
The microscopic study of heat expansion of monoclinic pepsin crystals was performed in temperature interval of -120 degrees C to +20 degrees C. The coefficient of heat expansion along the C axis was shown to be 8-10 times as large as along the B axis. This dynamics anisotropy is interpreted to reflect the domain mobility of the molecule.
在-120℃至+20℃的温度区间内对单斜晶型胃蛋白酶晶体的热膨胀进行了微观研究。结果表明,沿C轴的热膨胀系数比沿B轴的热膨胀系数大8至10倍。这种动力学各向异性被解释为反映了分子的结构域迁移率。