Mrevlishvili G M, Sharimanov Iu G
Biofizika. 1978 Mar-Apr;23(2):242-6.
Heat capacity and line width of proton magnetic resonance of collagen were studied by means of low-temperature calorimatry and high resolution NMR spectroscopy at different values of moisture in the temperature range of ice-water phase transition. Peculiarities of water phase transition in the presence of biopolymers were revealed. It was shown that a definite part of H2O in the "hydration layers" of the macromolecules (0.35 g of H2O/g of protein) is not transformed into ice even at a temperature decrease up to 4 K. The NMR data show that the total mobility of the bound water molecules remains high enough up to the water concentration at which the inner hydration layer of the macromolecule is formed. After the formation of hydrogen-bound water chains in the hydrate layers of collagen the mobility of the bound water molecules decreases.
在冰水相变温度范围内，通过低温量热法和高分辨率核磁共振光谱法，研究了不同湿度下胶原蛋白质子磁共振的热容和线宽。揭示了生物聚合物存在时水相转变的特性。结果表明，即使温度降至4K，大分子“水化层”中一定比例的H₂O（0.35g H₂O/g蛋白质）也不会转化为冰。核磁共振数据表明，在形成大分子内水化层的水浓度之前，结合水分子的总迁移率一直保持足够高。在胶原蛋白水合物层中形成氢键水链后，结合水分子的迁移率降低。
