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Synthetic peptide arrays for investigating protein interaction domains
Author(s) -
Volkmer Rudolf,
Tapia Victor,
Landgraf Christiane
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.04.028
Subject(s) - pdz domain , peptide , computational biology , domain (mathematical analysis) , sh3 domain , protein–protein interaction , synthetic biology , focus (optics) , yeast , nanotechnology , protein array analysis , peptide library , chemistry , computer science , biology , biochemistry , peptide sequence , gene , materials science , physics , signal transduction , mathematics , mathematical analysis , optics , proto oncogene tyrosine protein kinase src , gene expression , dna microarray
Synthetic peptide array technology was first developed in the early 1990s by Ronald Frank. Since then the technique has become a powerful tool for high throughput approaches in biology and biochemistry. Here, we focus on peptide arrays applied to investigate the binding specificity of protein interaction domains such as WW, SH3, and PDZ domains. We describe array‐based methods used to reveal domain networks in yeast, and briefly review rules as well as ideas about the synthesis and application of peptide arrays. We also provide initial results of a study designed to investigate the nature and evolution of SH3 domain interaction networks in eukaryotes.