Titlebook: Combinatorial Peptide Library Protocols; Shmuel Cabilly Book 1998 Humana Press 1998

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Introduction to Combinatorial Solid-Phase Assays for Enzyme Activity and Inhibition,ic enzymes has been expressed by the pharmaceutical industry, and the investment in the development of specific enzyme mhlbltors remains an important challenge. This chapter describes combinatorial approaches to the characterization of enzyme specificity and identification of enzyme inhibitors or le

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,Determination of Peptide Substrate Motifs for Protein Kinases Using a “One-Bead One-Compound” Combilation sites reported (.), and many protein kinases have been cloned and expressed. The sites of phosphorylation are usually serine, threonine, tyrosine, or occastonally histrdine. The two major classes of protein kinases are serme-threonine protein kmase and protein tyrosine kinase. Substrate motif

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Analysis of Protein Kinase Substrate Specificity by the Use of Peptide Libraries on Cellulose Papernases exhibit specificities that are often primarily determined by the amino acrds around the phosphorylation sites (.). Identification of amino acids that contribute to substrate motifs are essential for the understanding of signal transduction pathways and for the development of specific peptide s

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Generation of Multiuse Peptide Libraries for Functional Screenings,upporting matrix in a controlled manner so that fractions are available for multiple independent tests, free of interference from other constituents of the library. A method was developed to study the functional responses arlsing from individual constituent beads in a synthetic combinatorial peptide