Molecular basis for substrate specificity of protein kinases and phosphatases
β Scribed by John W. Sparks; David L. Brautigan
- Publisher
- Elsevier Science
- Year
- 1986
- Tongue
- English
- Weight
- 830 KB
- Volume
- 18
- Category
- Article
- ISSN
- 0020-711X
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Peptides, obtained by gradual removal of amino acids from both ends of pEKRPSQRSKYL, and stereoisomeric nonapeptides KRPSQRAKY with one D-amino acid residue successively in each position, were tested as substrates for protein kinase A. All these compounds were phosphorylated but at quite different r
A method is described for the elucidation of the peptide substrate phosphorylation specificity of a protein kinase. Peptide libraries with two to six degenerate positions and a length of seven or nine amino acids were generated directly on Sepharose beads by solidphase peptide synthesis according to