Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

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...

Topics

Adenosine Triphosphate
Adenylyl Imidodiphosphate
Bacterial Proteins
Chaperonin 10
Chaperonin 60
Dinucleoside Phosphates
Flow Injection Analysis
Heat-Shock Proteins
Mutation
Protein Denaturation
Protein Folding
Recombinant Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Ribonucleases

Source

Identifiers

PMID: 8103803
DOI: 10.1006/jmbi.1993.1471

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8103803-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

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

Refolding of barnase mutants and pro-barnase in the presence and absence of GroEL.Semantic proximity Read ↗

Folding of barnase in the presence of the molecular chaperone SecB.Semantic proximity Read ↗

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 ↗

⌁Select a neighboring publication to make it the new centre.