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- W2080426917 endingPage "62" @default.
- W2080426917 startingPage "55" @default.
- W2080426917 abstract "Once the sequence of a genome is in hand, understanding the function of its encoded proteins becomes a task of paramount importance. Much like the biochemists who first outlined different biochemical pathways, many genomic scientists are engaged in determining which proteins interact with which proteins, thereby establishing a protein interaction network. While these interactions have evolved in regard to their specificity, affinity and cellular function over billions of years, it is possible in the laboratory to isolate peptides from combinatorial libraries that bind to the same proteins with similar specificity, affinity and primary structures, which resemble those of the natural interacting proteins. We have termed this phenomenon 'convergent evolution'. In this review, we highlight various examples of convergent evolution that have been uncovered in experiments dissecting protein-protein interactions with combinatorial peptides. Thus, a fruitful approach for mapping protein-protein interactions is to isolate peptide ligands to a target protein and identify candidate interacting proteins in a sequenced genome by computer analysis." @default.
- W2080426917 created "2016-06-24" @default.
- W2080426917 creator A5000495048 @default.
- W2080426917 creator A5019046184 @default.
- W2080426917 creator A5033336232 @default.
- W2080426917 creator A5087592443 @default.
- W2080426917 date "2000-08-24" @default.
- W2080426917 modified "2023-10-06" @default.
- W2080426917 title "Convergent evolution with combinatorial peptides" @default.
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