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Article

Refolding of barnase in the presence of GroE.

Journal of molecular biology - 20 Aug 1993

Gray T E, Fersht A R

Abstract excerpt

The refolding of barnase in the presence of GroEL has been monitored on the millisecond to seconds time scale using stopped-flow kinetics. GroEL binds rapidly and tightly to the denatured enzyme with a second-order rate constant of greater than 1.3 x 10(8) s-1 M-1 and slows down greatly the rate of barnase refolding. However, addition of ever increasing concentrations of GroEL does not prevent barnase refolding...

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Source

Identifiers

PMID: 8103803
DOI: 10.1006/jmbi.1993.1471

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Refolding of barnase in the presence of GroE.PMID 8103803Read ↗

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The kinetic pathway of folding of barnase.Semantic proximity Read ↗

Transient folding intermediates characterized by protein engineering.Semantic proximity Read ↗

Lack of definable nucleation sites in the rate-limiting transition state of barnase under native conditions.Semantic proximity Read ↗

The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure.Semantic proximity Read ↗

Simulation of the diffusional association of barnase and barstar.Semantic proximity Read ↗

The role of Glu73 of barnase in catalysis and the binding of barstar.Semantic proximity Read ↗

Dynamic spin label study of the barstar-barnase complex.Semantic proximity Read ↗

Rapid, electrostatically assisted association of proteins.Semantic proximity Read ↗

Submillisecond events in protein folding.Semantic proximity Read ↗

Dynamics of the GroEL-protein complex: effects of nucleotides and folding mutants.Semantic proximity Read ↗

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