O'Neil K T, Erickson-Viitanen S, DeGrado W F
E. I. du Pont de Nemours & Company, Central Research and Development Department, Wilmington, Delaware 19880-0328.
J Biol Chem. 1989 Aug 25;264(24):14571-8.
A novel photoreactive amino acid has been incorporated synthetically into two model peptides and the calmodulin-binding domain from myosin light chain kinase. Cross-linked photoadducts of each peptide with calmodulin have been prepared and digested by chemical and/or enzymatic methods to determine the site of label attachment. Depending on the position of the photoprobe in the peptide sequence, either Met-144 or Met-71 is photolabeled. These results are discussed in relation to the three-dimensional structure of calmodulin obtained crystallographically and the known solution properties of calmodulin.
一种新型的光反应性氨基酸已被合成掺入到两种模型肽以及肌球蛋白轻链激酶的钙调蛋白结合结构域中。已制备了每种肽与钙调蛋白的交联光加合物，并通过化学和/或酶促方法进行消化，以确定标记附着的位点。根据光探针在肽序列中的位置，Met-144或Met-71被光标记。结合通过晶体学获得的钙调蛋白的三维结构以及钙调蛋白已知的溶液性质对这些结果进行了讨论。
