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Article

Low-stringency selection of TEM1 for BLIP shows interface plasticity and selection for faster binders.

Proceedings of the National Academy of Sciences of the United States of America - 27 Dec 2016

Cohen-Khait Ruth, Schreiber Gideon

Abstract excerpt

Protein-protein interactions occur via well-defined interfaces on the protein surface. Whereas the location of homologous interfaces is conserved, their composition varies, suggesting that multiple solutions may support high-affinity binding. In this study, we examined the plasticity of the interface of TEM1 β-lactamase with its protein inhibitor BLIP by low-stringency selection of a random TEM1 library using...

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Identifiers

PMID: 27956635
DOI: 10.1073/pnas.1613122113
PMCID: PMC5206572

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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