Buku A, Probst W C, Weiss K R, Heierhorst J
Department of Physiology and Biophysics, Mount Sinai School of Medicine, New York, New York 10029, USA.
Biochem Biophys Res Commun. 1996 Jan 26;218(3):854-9. doi: 10.1006/bbrc.1996.0152.
The calcium-dependent interaction of two synthetic peptides derived from the putative calmodulin-binding site in the protein kinase autoinhibitory region of twitchin was studied by fluorescence and CD spectroscopy. The peptides interacted with dansylcalmodulin in the presence of Ca2+ as shown by a change in the fluorescence emission spectra. Fluorescence titration of dansylcalmodulin with the peptides was used to quantify this interaction. The peptides appeared to assume a helical conformation in a non-polar environment as seen by CD spectroscopy. The ellipticity of Ca2+ calmodulin was enhanced in the presence of peptides compared with that of Ca2+ calmodulin and peptides alone, indicating that the peptides had formed a complex with calmodulin. These results support the assignment of the twitchin calmodulin-binding site.
通过荧光光谱和圆二色光谱研究了源自肌动蛋白激酶自抑制区域中假定钙调蛋白结合位点的两种合成肽的钙依赖性相互作用。如荧光发射光谱的变化所示，这些肽在Ca2+存在下与丹磺酰钙调蛋白相互作用。用肽对丹磺酰钙调蛋白进行荧光滴定以量化这种相互作用。如圆二色光谱所示，这些肽在非极性环境中似乎呈现螺旋构象。与单独的Ca2+钙调蛋白和肽相比，在肽存在下Ca2+钙调蛋白的椭圆率增加，表明这些肽已与钙调蛋白形成复合物。这些结果支持了肌动蛋白激酶钙调蛋白结合位点的归属。
