Controlled rotation of the F₁-ATPase reveals differential and continuous binding changes for ATP synthesis.
about
DNA replication at the single-molecule levelOperation mechanism of F(o) F(1)-adenosine triphosphate synthase revealed by its structure and dynamicsRotary catalysis of FoF1-ATP synthaseComparison between single-molecule and X-ray crystallography data on yeast F1-ATPaseOperating principles of rotary molecular motors: differences between F1 and V1 motorsF1-ATPase conformational cycle from simultaneous single-molecule FRET and rotation measurementsAnatomy of F1-ATPase powered rotationFrom self-sorted coordination libraries to networking nanoswitches for catalysis.Simple mechanism whereby the F1-ATPase motor rotates with near-perfect chemomechanical energy conversion.Theory for rates, equilibrium constants, and Brønsted slopes in F1-ATPase single molecule imaging experiments.Theory of single-molecule controlled rotation experiments, predictions, tests, and comparison with stalling experiments in F1-ATPaseChemomechanical coupling mechanism of F(1)-ATPase: catalysis and torque generation.Theory of long binding events in single-molecule-controlled rotation experiments on F1-ATPase.Timing of inorganic phosphate release modulates the catalytic activity of ATP-driven rotary motor proteinKinetics of nucleotide entry into RNA polymerase active site provides mechanism for efficiency and fidelity.Characterization of the temperature-sensitive reaction of F1-ATPase by using single-molecule manipulation.None of the rotor residues of F1-ATPase are essential for torque generation.Nonequilibrium dissipation-free transport in F₁-ATPase and the thermodynamic role of asymmetric allosterism.Torque transmission mechanism via DELSEED loop of F1-ATPase.Torque generation mechanism of F1-ATPase upon NTP binding.Power Stroke Angular Velocity Profiles of Archaeal A-ATP Synthase Versus Thermophilic and Mesophilic F-ATP Synthase Molecular Motors.What can be learned about the enzyme ATPase from single-molecule studies of its subunit F1?Essential Role of the ε Subunit for Reversible Chemo-Mechanical Coupling in F1-ATPase.Torque generation through the random movement of an asymmetric rotor: A potential rotational mechanism of the γ subunit of F(1)-ATPase.
P2860
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P2860
Controlled rotation of the F₁-ATPase reveals differential and continuous binding changes for ATP synthesis.
description
2012 nî lūn-bûn
@nan
2012 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Controlled rotation of the F₁- ...... ing changes for ATP synthesis.
@ast
Controlled rotation of the F₁- ...... ing changes for ATP synthesis.
@en
type
label
Controlled rotation of the F₁- ...... ing changes for ATP synthesis.
@ast
Controlled rotation of the F₁- ...... ing changes for ATP synthesis.
@en
prefLabel
Controlled rotation of the F₁- ...... ing changes for ATP synthesis.
@ast
Controlled rotation of the F₁- ...... ing changes for ATP synthesis.
@en
P2093
P2860
P356
P1476
Controlled rotation of the F₁- ...... ding changes for ATP synthesis
@en
P2093
Kazuhiko Kinosita
Kengo Adachi
Masasuke Yoshida
Takayuki Nishizaka
P2860
P2888
P356
10.1038/NCOMMS2026
P407
P577
2012-01-01T00:00:00Z
P5875
P6179
1000649040