Lovelady Heather H, Shashidhara Satish, Matthews W Garrett
Department of Physics, University of South Florida, Tampa, FL, 33620-5700.
Biopolymers. 2014 Apr;101(4):329-35. doi: 10.1002/bip.22365.
Type I collagen is a fibril-forming protein largely responsible for the mechanical stability of body tissues. The tissue level properties of collagen have been studied for decades, and an increasing number of studies have been performed at the fibril scale. However, the mechanical properties of collagen at the molecular scale are not well established. In the study presented herein, the persistence length of pepsin digested bovine type I collagen is extracted from the conformations assumed when deposited from solution onto two-dimensional surfaces. This persistence length is a measure of the flexibility of the molecule. Comparison of the results for molecules deposited from different solvents allows for the study of the effect of the solutions on the flexibility of the molecule and provides insight into the molecule's behavior in situ.
I型胶原蛋白是一种形成纤维的蛋白质,在很大程度上负责身体组织的机械稳定性。胶原蛋白的组织水平特性已经研究了几十年,并且在纤维尺度上进行的研究越来越多。然而,胶原蛋白在分子尺度上的力学性能尚未得到很好的确立。在本文提出的研究中,胃蛋白酶消化的牛I型胶原蛋白的持久长度是从其从溶液沉积到二维表面时所呈现的构象中提取出来的。这个持久长度是分子柔韧性的一种度量。比较从不同溶剂中沉积的分子的结果,可以研究溶液对分子柔韧性的影响,并深入了解分子在原位的行为。