Reverse engineering a protein: the mechanochemistry of ATP synthase.
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The unbinding of ATP from F1-ATPasePeriodic forces trigger knot untying during translocation of knotted proteins.The structure of the peripheral stalk of Thermus thermophilus H+-ATPase/synthaseLarge Terminase Conformational Change Induced by Connector Binding in Bacteriophage T7Making ATP.Rotation scheme of V1-motor is different from that of F1-motor.Simple models for extracting mechanical work from the ATP hydrolysis cycle.Intersubunit coordination in a homomeric ring ATPase.Anatomy of F1-ATPase powered rotationLinear analysis near a steady-state of biochemical networks: control analysis, correlation metrics and circuit theory.A computational analysis of ATP binding of SV40 large tumor antigen helicase motor.Mechanical operation and intersubunit coordination of ring-shaped molecular motors: insights from single-molecule studiesMonte Carlo modeling of single-molecule cytoplasmic dynein.Activation of pausing F1 motor by external forceModulation of mitochondrial proteome and improved mitochondrial function by biventricular pacing of dyssynchronous failing hearts.Cardiolipin: a proton trap for oxidative phosphorylation.Asymmetry in the F1-ATPase and its implications for the rotational cycle.ATP synthesis driven by proton transport in F1F0-ATP synthase.Zooming in on ATP hydrolysis in F1.Domain motion of individual F1-ATPase β-subunits during unbiased molecular dynamics simulations.Bending elasticity of anti-parallel beta-sheets.Quantitative proteomic analysis of dexamethasone-induced effects on osteoblast differentiation, proliferation, and apoptosis in MC3T3-E1 cells using SILAC.Theory for rates, equilibrium constants, and Brønsted slopes in F1-ATPase single molecule imaging experiments.Coupling of DNA unwinding to nucleotide hydrolysis in a ring-shaped helicase.Correlation between the conformational states of F1-ATPase as determined from its crystal structure and single-molecule rotationA comparative study of motor-protein motions by using a simple elastic-network model.Energy-driven subunit rotation at the interface between subunit a and the c oligomer in the F(O) sector of Escherichia coli ATP synthaseThermophilic ATP synthase has a decamer c-ring: indication of noninteger 10:3 H+/ATP ratio and permissive elastic coupling.A viral packaging motor varies its DNA rotation and step size to preserve subunit coordination as the capsid fillsTargeting mitochondrial function for the treatment of acute spinal cord injury.Structural divergence of the rotary ATPases.Single-molecule studies of viral DNA packaging.pH-dependent regulation of electron transport and ATP synthesis in chloroplasts.Stepping rotation of F(1)-ATPase with one, two, or three altered catalytic sites that bind ATP only slowly.Theory of long binding events in single-molecule-controlled rotation experiments on F1-ATPase.Catalytic robustness and torque generation of the F1-ATPaseDynamics and efficiency of Brownian rotors.On the structure of the stator of the mitochondrial ATP synthase.Single-molecule analysis of F0F1-ATP synthase inhibited by N,N-dicyclohexylcarbodiimidePrincipal role of the arginine finger in rotary catalysis of F1-ATPase.
P2860
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P2860
Reverse engineering a protein: the mechanochemistry of ATP synthase.
description
2000 nî lūn-bûn
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2000 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի մայիսին հրատարակված գիտական հոդված
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2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Reverse engineering a protein: the mechanochemistry of ATP synthase.
@ast
Reverse engineering a protein: the mechanochemistry of ATP synthase.
@en
type
label
Reverse engineering a protein: the mechanochemistry of ATP synthase.
@ast
Reverse engineering a protein: the mechanochemistry of ATP synthase.
@en
prefLabel
Reverse engineering a protein: the mechanochemistry of ATP synthase.
@ast
Reverse engineering a protein: the mechanochemistry of ATP synthase.
@en
P1476
Reverse engineering a protein: the mechanochemistry of ATP synthase.
@en
P304
P356
10.1016/S0005-2728(00)00096-7
P407
P577
2000-05-01T00:00:00Z