Back to Search
Start Over
Calmodulin interacts with amphiphilic peptides composed of all D-amino acids
- Source :
- Nature. April 14, 1994, Vol. 368 Issue 6472, p651, 3 p.
- Publication Year :
- 1994
-
Abstract
- Use of melittin and RS20 that contain only D-amino acids indicates that calmodulin binds avidly to both, revealing the high sterical tolerance of the calmodulin-peptide binding surface. This may lead to the development of non- or slowly-hydrolysable calmodulin inhibitors that function at the intracellular level. The binding site is the same as that for peptides possessing L-amino acids.
Details
- ISSN :
- 00280836
- Volume :
- 368
- Issue :
- 6472
- Database :
- Gale General OneFile
- Journal :
- Nature
- Publication Type :
- Academic Journal
- Accession number :
- edsgcl.15469385