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 energetics of F1-ATPase motor.

Biophysical journal - 1 Mar 2007

Muneyuki Eiro, Watanabe-Nakayama Takahiro, Suzuki Tetsuya, Yoshida Masasuke, Nishizaka Takayuki, Noji Hiroyuki

Abstract excerpt

Motor proteins are essential in life processes because they convert the free energy of ATP hydrolysis to mechanical work. However, the fundamental question on how they work when different amounts of free energy are released after ATP hydrolysis remains unanswered. To answer this question, it is essential to clarify how the stepping motion of a motor protein reflects the concentrations of ATP, ADP, and P(i) in its...

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 Bacillus
Share to Bacterial Proteins

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

Share to Hydrolysis

Share to Models, Molecular

Share to Molecular Motor Proteins

Share to Motion

Share to Proton-Translocating ATPases

Source

Open in PubMed Open full text

Identifiers

PMID: 17158579
DOI: 10.1529/biophysj.106.097170
PMCID: PMC1796807

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 energetics of F1-ATPase motor.PMID 17158579Read ↗

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

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

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

Torque generation and utilization in motor enzyme F0F1-ATP synthase: half-torque F1 with short-sized pushrod helix and reduced ATP Synthesis by half-torque F0F1.Semantic proximity Read ↗

Two rotary motors in F-ATP synthase are elastically coupled by a flexible rotor and a stiff stator stalk.Semantic proximity Read ↗

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

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

The F subunit of Thermus thermophilus V1-ATPase promotes ATPase activity but is not necessary for rotation.Semantic proximity Read ↗

Synthase (H(+) ATPase): coupling between catalysis, mechanical work, and proton translocation.Semantic proximity Read ↗

36 degrees step size of proton-driven c-ring rotation in FoF1-ATP synthase.Semantic proximity Read ↗

Roles of the beta subunit hinge domain in ATP synthase F(1) sector: hydrophobic network formed by introduced betaPhe174 inhibits subunit rotation.Semantic proximity Read ↗

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