The heat released during catalytic turnover enhances the diffusion of an enzyme.
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Enzyme Catalysis To Power Micro/NanomachinesImpulsive Enzymes: A New Force in MechanobiologyThe Physics and Physical Chemistry of Molecular Machines.Perspective: Watching low-frequency vibrations of water in biomolecular recognition by THz spectroscopy.ATP Hydrolysis Induced Conformational Changes in the Vitamin B12 Transporter BtuCD Revealed by MD Simulations.Activated kinetics in a nonequilibrium thermal bath.Quantitative determination of ribosome nascent chain stability.Probing conformational dynamics of an enzymatic active site by an in situ single fluorogenic probe under piconewton force manipulation.Self-propulsion and interactions of catalytic particles in a chemically active medium.Materials learning from life: concepts for active, adaptive and autonomous molecular systems.Hydrogen-Deuterium Exchange of Lipoxygenase Uncovers a Relationship between Distal, Solvent Exposed Protein Motions and the Thermal Activation Barrier for Catalytic Proton-Coupled Electron Tunneling.Temperature-Jump Fluorescence Provides Evidence for Fully Reversible Microsecond Dynamics in a Thermophilic Alcohol Dehydrogenase.Measurement of Rapid Protein Diffusion in the Cytoplasm by Photo-Converted Intensity Profile Expansion.Of capturing fish, mobilizing enzymes, and a surprising source for serotonin.An in vitro tag-and-modify protein sample generation method for single-molecule fluorescence resonance energy transfer.Universal glass-forming behavior of in vitro and living cytoplasm.Enzyme leaps fuel antichemotaxis.Synthetic, Switchable Enzymes.Directional Force Originating from ATP Hydrolysis Drives the GroEL Conformational Change.Catalysis-Driven Self-Thermophoresis of Janus Plasmonic Nanomotors.Reentrant Phase Transitions and Non-Equilibrium Dynamics in Membraneless Organelles.Optical vs. chemical driving for molecular machines.Substrate-driven chemotactic assembly in an enzyme cascade.Motor-like Properties of Nonmotor Enzymes.Force Spectrum Microscopy Using Mitochondrial Fluctuations of Control and ATP-Depleted Cells
P2860
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P2860
The heat released during catalytic turnover enhances the diffusion of an enzyme.
description
2014 nî lūn-bûn
@nan
2014 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
The heat released during catalytic turnover enhances the diffusion of an enzyme.
@ast
The heat released during catalytic turnover enhances the diffusion of an enzyme.
@en
type
label
The heat released during catalytic turnover enhances the diffusion of an enzyme.
@ast
The heat released during catalytic turnover enhances the diffusion of an enzyme.
@en
prefLabel
The heat released during catalytic turnover enhances the diffusion of an enzyme.
@ast
The heat released during catalytic turnover enhances the diffusion of an enzyme.
@en
P2093
P2860
P50
P356
P1433
P1476
The heat released during catalytic turnover enhances the diffusion of an enzyme
@en
P2093
Christian A M Wilson
Clement Riedel
Ronen Gabizon
Steve Pressé
Susan Marqusee
P2860
P2888
P304
P356
10.1038/NATURE14043
P407
P577
2014-12-10T00:00:00Z
P6179
1023720213