How calmodulin binds its targets: sequence independent recognition of amphiphilic alpha-helices

Trends Biochem Sci. 1990 Feb;15(2):59-64. doi: 10.1016/0968-0004(90)90177-d.


Calmodulin (CaM) is a protein capable of recognizing positively charged, amphiphilic alpha-helical peptides independent of their precise amino acid sequences; this structural feature has also been found in many CaM-binding proteins. Recent work involving crystallography and site-directed mutagenesis of CaM along with studies of photoreactive and fluorescent CaM-binding peptides have helped define how calmodulin interacts with amphiphilic helices.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Calmodulin / metabolism*
  • Calmodulin-Binding Proteins / metabolism
  • Methionine / metabolism
  • Molecular Sequence Data
  • Protein Conformation


  • Calmodulin
  • Calmodulin-Binding Proteins
  • Methionine