Reducing a CO to a CH 2 moiety in a peptide bond destroys the ability of the peptide link to act as a proton acceptor in a hydrogen-bonded structure. Here, this modification is introduced into different positions of the helical peptide, acetyl-WGG(RAAAA) 4 R-amide, and the melting of these peptides
Effect on protein phosphatase activity of peptide backbone modification and truncation of the autoinhibitory domain peptide of calcineurin
โ Scribed by BANNOW, CAROL A. ;STAPLES, DOUGLAS J. ;SMITH, CLARK W. ;CHAPMAN, DARRYL L. ;LEACH, KAREN L.
- Book ID
- 115099861
- Publisher
- Wiley (Blackwell Publishing)
- Year
- 2009
- Tongue
- English
- Weight
- 408 KB
- Volume
- 47
- Category
- Article
- ISSN
- 0367-8377
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## Abstract ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF.
The effects of divalent metals, metal chelators (EDTA, EGTA) and sodium dodecyl sulfate were investigated on the phosphatase activity of isolated bovine brain calcineurin assayed in the absence (called intrinsic) and presence of calmodulin. Intrinsic phosphatase was increased by Mn2+, was unaffected