天然胶原纤维体外组装的热力学研究。
Thermodynamic studies of the assembly in vitro of native collagen fibrils.
作者信息
Cooper A
出版信息
Biochem J. 1970 Jul;118(3):355-65. doi: 10.1042/bj1180355.
Abstract
Measurements of the solubility of calf-skin tropocollagen in neutral phosphate buffers in the temperature range 20-37 degrees C show that native collagen fibril formation is an endothermic process made thermodynamically favourable by a large positive entropy of precipitation associated with structural changes in the surrounding solvent. The effect of inorganic ions and small solute molecules on precipitation seems to be correlated with their structural effects on liquid water. Heterogeneity in the precipitation properties of the collagen solutions may be related to changes in the configurational entropy of the macromolecules due to intramolecular cross-linking.
摘要
对小牛皮原胶原蛋白在20至37摄氏度的中性磷酸盐缓冲液中的溶解度进行测量，结果表明天然胶原纤维的形成是一个吸热过程，周围溶剂结构变化所伴随的大量正沉淀熵使其在热力学上变得有利。无机离子和小溶质分子对沉淀的影响似乎与其对液态水的结构影响相关。胶原溶液沉淀特性的异质性可能与分子内交联导致的大分子构型熵的变化有关。
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