Fluorescence Properties of Calmodulin-Binding Peptides Reflect Alpha-Helical Periodicity
- 12 June 1987
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 236 (4807) , 1454-1456
- https://doi.org/10.1126/science.3589665
Abstract
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.This publication has 14 references indexed in Scilit:
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