| Literature DB >> 6326527 |
M Sellinger-Barnette, B Weiss.
Abstract
In summary, we have demonstrated the existence of several endogenous substances capable of inhibiting the action of calmodulin and have identified certain structural features of a peptide that confer calmodulin inhibitory activity. These include a net positive charge, a region of hydrophobic amino acids, and the ability to form a hydrophobic alpha-helix. We believe that these properties can be used to predict the calmodulin inhibitory potency of other peptides and can also provide an insight into the structural characteristics present in calmodulin-sensitive enzymes.Entities:
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Year: 1984 PMID: 6326527
Source DB: PubMed Journal: Adv Cyclic Nucleotide Protein Phosphorylation Res ISSN: 0747-7767