Synthetic peptide arrays for investigating protein interaction domains

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 intera...

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Bibliographic Details
Published inFEBS letters Vol. 586; no. 17; pp. 2780 - 2786
Main Authors Volkmer, Rudolf, Tapia, Victor, Landgraf, Christiane
Format Journal Article
LanguageEnglish
Published England Elsevier B.V 14.08.2012
Subjects
Animals
Biochemistry - methods
Cellulose - chemistry
Equipment Design
Fungal Proteins - chemistry
Humans
PDZ domains
Peptide arrays
Peptide Library
Peptides - chemistry
Protein Array Analysis - methods
Protein Binding
Protein interaction domains
Protein Interaction Domains and Motifs
Protein Interaction Mapping - methods
Protein Structure, Tertiary
SH3 domains
SPOT synthesis
WW domains
PDZ domains
SH3 domains
SPOT synthesis
WW domains
Peptide arrays
Protein interaction domains
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Summary: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.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
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ObjectType-Review-1
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2012.04.028