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Science 12 June 1987:
Vol. 236. no. 4807, pp. 1454 - 1456
DOI: 10.1126/science.3589665
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Articles

Science, Vol 236, Issue 4807, 1454-1456
Copyright © 1987 by American Association for the Advancement of Science

articles

Fluorescence properties of calmodulin-binding peptides reflect alpha-helical periodicity

KT O'Neil, HR Wolfe Jr, S Erickson-Viitanen, and WF DeGrado

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.


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