Sellinger-Barnette M, Weiss B
Adv Cyclic Nucleotide Protein Phosphorylation Res. 1984;16:261-76.
In summary, we have demonstrated the existence of several endogenous substances capable of inhibiting the action of calmodulin and have identified certain structural features of a peptide that confer calmodulin inhibitory activity. These include a net positive charge, a region of hydrophobic amino acids, and the ability to form a hydrophobic alpha-helix. We believe that these properties can be used to predict the calmodulin inhibitory potency of other peptides and can also provide an insight into the structural characteristics present in calmodulin-sensitive enzymes.
总之，我们已经证明了几种能够抑制钙调蛋白作用的内源性物质的存在，并确定了赋予钙调蛋白抑制活性的肽的某些结构特征。这些特征包括净正电荷、疏水氨基酸区域以及形成疏水α螺旋的能力。我们认为，这些特性可用于预测其他肽的钙调蛋白抑制效力，还能深入了解钙调蛋白敏感酶中存在的结构特征。
