title: Interaction of various peptides with calmodulin.
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.
mesh_terms: D015105:3',5'-Cyclic-AMP Phosphodiesterases / Q000378:metabolism*; D000818:Animals; D001921:Brain / Q000201:enzymology; D002147:Calmodulin / Q000378:metabolism* / Q000494:pharmacology; D004723:Endorphins / Q000494:pharmacology; D009419:Nerve Tissue Proteins / Q000494:pharmacology; D010455:Peptides / Q000378:metabolism* / Q000494:pharmacology; D011485:Protein Binding
chemical_list: D002147:Calmodulin; D004723:Endorphins; D009419:Nerve Tissue Proteins; D010455:Peptides; D015105:3',5'-Cyclic-AMP Phosphodiesterases