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Article

How optimal are the binding energetics of barnase and barstar?

Biophysical journal - 1 Sept 2004

Wang Ting, Tomic Sanja, Gabdoulline Razif R, Wade Rebecca C

Abstract excerpt

The extracellular ribonuclease barnase and its intracellular inhibitor barstar bind fast and with high affinity. Although extensive experimental and theoretical studies have been carried out on this system, it is unclear what the relative importance of different contributions to the high affinity...

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Identifiers

PMID: 15345541
DOI: 10.1529/biophysj.104.040964
PMCID: PMC1304567

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-15345541-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

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How optimal are the binding energetics of barnase and barstar?PMID 15345541Read ↗

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Experimental assignment of the structure of the transition state for the association of barnase and barstar.Semantic proximity Read ↗

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Barnase-Barstar: from first encounter to final complex.Semantic proximity Read ↗

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