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

Single-molecule analysis of the rotation of F₁-ATPase under high hydrostatic pressure.

Biophysical journal - 1 Oct 2013

Okuno Daichi, Nishiyama Masayoshi, Noji Hiroyuki

Abstract excerpt

F1-ATPase is the water-soluble part of ATP synthase and is an ATP-driven rotary molecular motor that rotates the rotary shaft against the surrounding stator ring, hydrolyzing ATP. Although the mechanochemical coupling mechanism of F1-ATPase has been well studied, the molecular details of individual reaction steps remain unclear. In this study, we conducted a single-molecule rotation assay of F1 from thermophilic...

Read the complete abstract on PubMed

Topics

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

Share to Bacillus
Share to Bacterial Proteins
Share to Hydrostatic Pressure

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Kinetics

Share to Mutation

Share to Protein Binding

Share to Proton-Translocating ATPases

Share to Rotation

Source

Open in PubMed Open full text

Identifiers

PMID: 24094404
DOI: 10.1016/j.bpj.2013.08.036
PMCID: PMC3822718

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Single-molecule analysis of the rotation of F₁-ATPase under high hydrostatic pressure.PMID 24094404Read ↗

Rotary catalysis of bovine mitochondrial F1-ATPase studied by single-molecule experiments.Semantic proximity Read ↗

A structure-based model for the synthesis and hydrolysis of ATP by F1-ATPase.Semantic proximity Read ↗

Correlation between the conformational states of F1-ATPase as determined from its crystal structure and single-molecule rotation.Semantic proximity Read ↗

Temperature dependence of single molecule rotation of the Escherichia coli ATP synthase F1 sector reveals the importance of gamma-beta subunit interactions in the catalytic dwell.Semantic proximity Read ↗

Single molecule energetics of F1-ATPase motor.Semantic proximity Read ↗

Molecular mechanism of ATP hydrolysis in F1-ATPase revealed by molecular simulations and single-molecule observations.Semantic proximity Read ↗

The six steps of the complete F1-ATPase rotary catalytic cycle.Semantic proximity Read ↗

Role of α/β interface in F1 ATPase rotational catalysis probed by inhibitors and mutations.Semantic proximity Read ↗

None of the rotor residues of F1-ATPase are essential for torque generation.Semantic proximity Read ↗

Comparison between single-molecule and X-ray crystallography data on yeast F1-ATPase.Semantic proximity Read ↗

Stochastic rotational catalysis of proton pumping F-ATPase.Semantic proximity Read ↗

ATP hydrolysis and synthesis of a rotary motor V-ATPase from Thermus thermophilus.Semantic proximity Read ↗

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