O'Neil K T, Wolfe H R, Erickson-Viitanen S, DeGrado W F
Science. 1987 Jun 12;236(4807):1454-6. doi: 10.1126/science.3589665.
A basic amphiphilic alpha-helix is a structural feature common to many calmodulin-binding peptides and proteins. A set of fluorescent analogues of a very tight binding inhibitor (dissociation constant of 200 picomolar) of calmodulin has been synthesized. The fluorescent amino acid tryptophan has been systematically moved throughout the sequence of this peptide. The fluorescence properties for the peptides repeat every three to four residues and are consistent with the periodicity observed for an alpha-helix.
一种基本的两亲性α-螺旋是许多钙调蛋白结合肽和蛋白质共有的结构特征。已合成了一组钙调蛋白紧密结合抑制剂（解离常数为200皮摩尔）的荧光类似物。荧光氨基酸色氨酸已在该肽的整个序列中系统地移动。这些肽的荧光特性每三到四个残基重复一次，与α-螺旋观察到的周期性一致。
