钙调蛋白如何结合其靶标：两亲性α螺旋的序列非依赖性识别。
How calmodulin binds its targets: sequence independent recognition of amphiphilic alpha-helices.
作者信息
O'Neil K T, DeGrado W F
机构信息
E. I. du Pont de Nemours & Co., Central Research and Development Department, Wilmington, DE 19880-0328.
出版信息
Trends Biochem Sci. 1990 Feb;15(2):59-64. doi: 10.1016/0968-0004(90)90177-d.
Calmodulin (CaM) is a protein capable of recognizing positively charged, amphiphilic alpha-helical peptides independent of their precise amino acid sequences; this structural feature has also been found in many CaM-binding proteins. Recent work involving crystallography and site-directed mutagenesis of CaM along with studies of photoreactive and fluorescent CaM-binding peptides have helped define how calmodulin interacts with amphiphilic helices.
钙调蛋白（CaM）是一种能够识别带正电荷的两亲性α-螺旋肽的蛋白质，而不依赖于其精确的氨基酸序列；这种结构特征在许多钙调蛋白结合蛋白中也有发现。最近涉及钙调蛋白晶体学和定点诱变的研究，以及对光反应性和荧光性钙调蛋白结合肽的研究，有助于确定钙调蛋白与两亲性螺旋的相互作用方式。
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