del Pozo A M, Olmo N, Oñaderra M, Lizarbe M A, Gavilanes J G
Int J Pept Protein Res. 1986 Aug;28(2):173-8. doi: 10.1111/j.1399-3011.1986.tb03244.x.
The existence of a hydrophobic cluster on the COOH-telopeptides of type I collagen has been observed by studies on the binding of 1-anilinonaphthalene-8-sulfonic acid (ANS) to this protein. Collagen contains one binding site for the fluorescent probe. This hydrophobic cluster remains after pepsin digestion thus indicating that it is formed by the undegraded portions of the COOH-extrahelical ends of the protein. Energy transfer from tyrosine to ANS has been observed. The triple helix of collagen does not bind ANS.
通过对1-苯胺基萘-8-磺酸（ANS）与该蛋白质结合的研究，已观察到I型胶原蛋白的COOH-端肽上存在疏水簇。胶原蛋白含有一个荧光探针结合位点。胃蛋白酶消化后该疏水簇仍然存在，这表明它是由蛋白质COOH-螺旋外端未降解部分形成的。已观察到从酪氨酸到ANS的能量转移。胶原蛋白的三螺旋不结合ANS。
