Journal article
Interaction of various peptides with calmodulin
Advances in cyclic nucleotide and protein phosphorylation research, v 16
01 Jan 1984
PMID: 6326527
Featured in Collection : UN Sustainable Development Goals @ Drexel
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.
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Details
- Title
- Interaction of various peptides with calmodulin
- Creators
- M Sellinger-BarnetteB Weiss
- Publication Details
- Advances in cyclic nucleotide and protein phosphorylation research, v 16
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Pharmacology and Physiology
- Web of Science ID
- WOS:A1984AAB0400020
- Scopus ID
- 2-s2.0-0021296413
- Other Identifier
- 991019184305804721
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Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Biochemistry & Molecular Biology