Discover Community Create You

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

Modeling Hsp70-mediated protein folding.

Biophysical journal - 15 Jul 2006

Hu Bin, Mayer Matthias P, Tomita Masaru

Abstract excerpt

The Hsp70 chaperone system is the major molecular chaperone system that assists protein-folding processes in all cells. To understand these processes, we analyzed the kinetic characteristics of the Escherichia coli homologs of this chaperone system during folding of a denatured protein using computer simulations and compared the results with in vitro refolding experiments. Rate constants used for the model were...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adenosine Triphosphate
Share to Computer Simulation
Share to Escherichia coli Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HSP70 Heat-Shock Proteins

Share to Models, Biological

Share to Mutation

Share to Protein Folding

Source

Open in PubMed Open full text

Identifiers

PMID: 16648174
DOI: 10.1529/biophysj.106.083394
PMCID: PMC1483108

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Modeling Hsp70-mediated protein folding.PMID 16648174Read ↗

Influence of molecular and chemical chaperones on protein foldingSemantic proximity Read ↗

Key residues involved in Hsp70 regulatory activity and affect of co-chaperones on mechanism of action.Semantic proximity Read ↗

Disaggregating chaperones: an unfolding story.Semantic proximity Read ↗

Probing the different chaperone activities of the bacterial HSP70-HSP40 system using a thermolabile luciferase substrate.Semantic proximity Read ↗

Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones.Semantic proximity Read ↗

Chaperonin-assisted protein folding: a chronologue.Semantic proximity Read ↗

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

Mutagenesis reveals the complex relationships between ATPase rate and the chaperone activities of Escherichia coli heat shock protein 70 (Hsp70/DnaK).Semantic proximity Read ↗

Binding and folding: in search of intramolecular chaperone-like building block fragments.Semantic proximity Read ↗

Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli.Semantic proximity Read ↗

Conformational equilibria in allosteric control of Hsp70 chaperones.Semantic proximity Read ↗

[Analysing protein folding transition state using protein engineering].Semantic proximity Read ↗

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