Steiner R F, Marshall L, Needleman D
Arch Biochem Biophys. 1986 Apr;246(1):286-300. doi: 10.1016/0003-9861(86)90474-1.
Melittin has been found to interact with both the N- and C-terminal half-molecules of calmodulin, as well as the intact molecule, in the presence of Ca2+. The interaction results in a major change in the microenvironment of Trp-19, which is in a more nonpolar, solvent-shielded, and immobilized microenvironment in the complex. The properties of Tyr-99 and Tyr-138 of calmodulin are altered by complex formation. From measurements of the efficiencies of radiationless energy transfer from Trp-19 to the nitro derivatives of Tyr-99 and/or Tyr-138, it is concluded that Trp-19 is located in proximity to the C-terminal lobe of calmodulin in the complex.
已发现蜂毒肽在Ca2+存在的情况下，能与钙调蛋白的N端和C端半分子以及完整分子相互作用。这种相互作用导致色氨酸-19微环境发生重大变化，在复合物中色氨酸-19处于更非极性、溶剂屏蔽且固定的微环境中。钙调蛋白的酪氨酸-99和酪氨酸-138的性质因复合物形成而改变。通过测量从色氨酸-19到酪氨酸-99和/或酪氨酸-138硝基衍生物的无辐射能量转移效率得出结论，在复合物中色氨酸-19位于钙调蛋白C端叶附近。
