Renugopalakrishnan V, Carreira L A, Collette T W, Dobbs J C, Chandraksasan G, Lord R C
Harvard Medical School, Boston, MA 02115, USA.
Z Naturforsch C J Biosci. 1998 May-Jun;53(5-6):383-8. doi: 10.1515/znc-1998-5-613.
The individual chains in the triple helix of collagen occur in a conformation related to polyproline II because of the presence of large number of imino peptide bonds. However, these residues are not evenly distributed in the collagen molecule which also contains many non-imino residues. These non-imino regions of collagen may be expected to show preference for other than triple helical conformations. The appearance of several Raman bands in solution phase at 65 degrees C raises the possibility of non-uniform triple helical structure in collagen. Raman spectroscopic studies on collagen in the solid state and in solution at a temperature greater than its denaturation temperature, reported here suggest that denatured collagen may exhibit an ensemble of conformational states with yet unknown implications to the biochemical interactions of this important protein component of connective tissues.
由于存在大量亚氨基肽键，胶原蛋白三螺旋中的各个链呈现出与聚脯氨酸II相关的构象。然而，这些残基在胶原蛋白分子中分布并不均匀，该分子还包含许多非亚氨基残基。胶原蛋白的这些非亚氨基区域可能倾向于呈现除三螺旋构象之外的其他构象。在65摄氏度的溶液相中出现的几个拉曼谱带增加了胶原蛋白中存在非均匀三螺旋结构的可能性。本文报道的对固态和高于其变性温度的溶液中的胶原蛋白进行的拉曼光谱研究表明，变性胶原蛋白可能呈现出一系列构象状态，这对结缔组织中这种重要蛋白质成分的生化相互作用的影响尚不清楚。
