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doi: 10.1038/71951
pmid: 10625395
Peptide-binding ligands would be useful for directing reagents to particular epitopes in a protein, the detection of peptide hormones, and many other applications. Here we show that peptides of modest size isolated from a library using a simple genetic assay can act as specific receptors for other peptides. The equilibrium dissociation constants of these peptide-peptide complexes are higher than those of typical monoclonal antibody-epitope complexes. Nonetheless, as shown here, these peptide-binding peptides can be used to detect or purify proteins containing the partner peptide.
Binding Sites, Operator Regions, Genetic, Blotting, Western, Molecular Sequence Data, Ligands, Chromatography, Affinity, DNA-Binding Proteins, Epitopes, Lac Operon, Genes, Reporter, Peptide Library, Escherichia coli, Animals, Humans, Amino Acid Sequence, Cloning, Molecular, Insulin-Like Growth Factor I, Chickens, Dimerization, Interleukin-1
Binding Sites, Operator Regions, Genetic, Blotting, Western, Molecular Sequence Data, Ligands, Chromatography, Affinity, DNA-Binding Proteins, Epitopes, Lac Operon, Genes, Reporter, Peptide Library, Escherichia coli, Animals, Humans, Amino Acid Sequence, Cloning, Molecular, Insulin-Like Growth Factor I, Chickens, Dimerization, Interleukin-1
citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 42 | |
popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Top 10% | |
influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Top 10% | |
impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 10% |