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  • Title: Studies of the calmodulin-binding site of twitchin with synthetic peptides using fluorescence and CD spectroscopy.
    Author: Buku A, Probst WC, Weiss KR, Heierhorst J.
    Journal: Biochem Biophys Res Commun; 1996 Jan 26; 218(3):854-9. PubMed ID: 8579604.
    Abstract:
    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.
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