scholarly journals Quantifying the Heat Dissipation from Molecular Motor’s Transport Properties in Nonequilibrium Steady States

2016 ◽  
Author(s):  
Wonseok Hwang ◽  
Changbong Hyeon
Keyword(s):  
Single Molecule ◽  
Molecular Motors ◽  
Heat Dissipation ◽  
Molecular Motor ◽  
Diffusion Constant ◽  
Nonequilibrium Steady States ◽  
Directed Motion ◽  
Mean Velocity ◽  
Self Diffusion ◽  
Brownian Particles

Theoretical analysis, which maps single molecule time trajectories of a molecular motor onto unicyclic Markov processes, allows us to evaluate the heat dissipated from the motor and to elucidate its dependence on the mean velocity and diffusivity. Unlike passive Brownian particles in equilibrium, the velocity and diffusion constant of molecular motors are closely inter-related to each other. In particular, our study makes it clear that the increase of diffusivity with the heat production is a natural outcome of active particles, which is reminiscent of the recent experimental premise that the diffusion of an exothermic enzyme is enhanced by the heat released from its own catalytic turnover. Compared with freely diffusing exothermic enzymes, kinesin-1 whose dynamics is confined on one-dimensional tracks is highly efficient in transforming conformational fluctuations into a locally directed motion, thus displaying a significantly higher enhancement in diffusivity with its turnover rate. Putting molecular motors and freely diffusing enzymes on an equal footing, our study offers thermodynamic basis to understand the heat enhanced self-diffusion of exothermic enzymes.

scholarly journals A model of processive walking and slipping of kinesin-8 molecular motors

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Ping Xie
Keyword(s):  
Single Molecule ◽  
Molecular Motors ◽  
External Load ◽  
Molecular Motor ◽  
Velocity Versus ◽  
Stick Slip ◽  
Load Dependence ◽  
Chemomechanical Coupling ◽  
Similarities And Differences ◽  
Stick Slip Motion

AbstractKinesin-8 molecular motor can move with superprocessivity on microtubules towards the plus end by hydrolyzing ATP molecules, depolymerizing microtubules. The available single molecule data for yeast kinesin-8 (Kip3) motor showed that its superprocessive movement is frequently interrupted by brief stick–slip motion. Here, a model is presented for the chemomechanical coupling of the kinesin-8 motor. On the basis of the model, the dynamics of Kip3 motor is studied analytically. The analytical results reproduce quantitatively the available single molecule data on velocity without including the slip and that with including the slip versus external load at saturating ATP as well as slipping velocity versus external load at saturating ADP and no ATP. Predicted results on load dependence of stepping ratio at saturating ATP and load dependence of velocity at non-saturating ATP are provided. Similarities and differences between dynamics of kinesin-8 and that of kinesin-1 are discussed.

DIRECTED MOTION OF BROWNIAN MOTORS: A RATCHET MODEL OF TWO-COUPLED MOLECULAR MOTORS

2007 ◽  
Vol 21 (28) ◽  
pp. 1915-1921 ◽  
Author(s):  
SHUTANG WEN ◽  
HONGWEI ZHANG ◽  
LEIAN LIU ◽  
XIAOFENG SUN ◽  
YUXIAO LI
Keyword(s):  
Molecular Motors ◽  
Particle System ◽  
Langevin Equations ◽  
Transition Rates ◽  
Neck Length ◽  
Directed Motion ◽  
Mean Velocity ◽  
Positive Direction ◽  
Brownian Motors ◽  
The Individual

We investigated the motion of two-head Brownian motors by introducing a model in which the two heads coupled through an elastic spring is subjected to a stochastic flashing potential. The ratchet potential felt by the individual head is anti-correlated. The mean velocity was calculated based on Langevin equations. It turns out that we can obtain a unidirectional current. The current is sensitive to the transition rates and neck length and other parameters. The coupling of transition rate and neck length leads to variations both in the values and directions of currency. With a larger neck length, the bi-particle system has a larger velocity in one direction, while with a smaller neck length, it has a smaller velocity in the other direction. This is very likely the case of myosins with a larger neck length and larger velocity in the positive direction of filaments and kinesins with a smaller neck length and smaller velocity in the negative direction of microtubules. We also further investigated how current reversal depended on the neck length and the transition rates.

Molecular Motors: Force and Movement Generated by Single Myosin II Molecules

Physiology ◽  
2002 ◽  
Vol 17 (5) ◽  
pp. 213-218 ◽  
Author(s):  
Caspar Rüegg ◽  
Claudia Veigel ◽  
Justin E. Molloy ◽  
Stephan Schmitz ◽  
John C. Sparrow ◽  
...  
Keyword(s):  
Optical Tweezers ◽  
Single Molecule ◽  
Molecular Motors ◽  
Molecular Motor ◽  
Myosin Ii ◽  
Force Production ◽  
Myosin Isoforms ◽  
Single Molecule Level ◽  
Recent Developments ◽  
Muscle Myosin

Muscle myosin II is an ATP-driven, actin-based molecular motor. Recent developments in optical tweezers technology have made it possible to study movement and force production on the single-molecule level and to find out how different myosin isoforms may have adapted to their specific physiological roles.

Single-molecule mechanical study of an autonomous artificial translational molecular motor beyond bridge-burning design

Nanoscale ◽  
2021 ◽  
Author(s):  
Xinpeng Hu ◽  
Xiaodan Zhao ◽  
Iong Ying Loh ◽  
Jie Yan ◽  
Zhisong Wang
Keyword(s):  
Single Molecule ◽  
Molecular Motors ◽  
Molecular Motor ◽  
Force Generation ◽  
Single Motor ◽  
Mechanical Study

A key capability of molecular motors is sustainable force generation by a single motor copy. Direct force characterization at single-motor level is still missing for artificial molecular motors, though long...

scholarly journals Molecular motor crossing the frontier of classical to quantum tunneling motion

2020 ◽  
Vol 117 (26) ◽  
pp. 14838-14842 ◽  
Author(s):  
Samuel Stolz ◽  
Oliver Gröning ◽  
Jan Prinz ◽  
Harald Brune ◽  
Roland Widmer
Keyword(s):  
Bias Voltage ◽  
Molecular Motors ◽  
Quantum Tunneling ◽  
Molecular Motor ◽  
Scanning Tunneling ◽  
Inelastic Electron ◽  
Directed Motion ◽  
Tunneling Microscopy ◽  
Nonequilibrium Processes ◽  
Classical Motion

The reliability by which molecular motor proteins convert undirected energy input into directed motion or transport has inspired the design of innumerable artificial molecular motors. We have realized and investigated an artificial molecular motor applying scanning tunneling microscopy (STM), which consists of a single acetylene (C2H2) rotor anchored to a chiral atomic cluster provided by a PdGa(111) surface that acts as a stator. By breaking spatial inversion symmetry, the stator defines the unique sense of rotation. While thermally activated motion is nondirected, inelastic electron tunneling triggers rotations, where the degree of directionality depends on the magnitude of the STM bias voltage. Below 17 K and 30-mV bias voltage, a constant rotation frequency is observed which bears the fundamental characteristics of quantum tunneling. The concomitantly high directionality, exceeding 97%, implicates the combination of quantum and nonequilibrium processes in this regime, being the hallmark of macroscopic quantum tunneling. The acetylene on PdGa(111) motor therefore pushes molecular machines to their extreme limits, not just in terms of size, but also regarding structural precision, degree of directionality, and cross-over from classical motion to quantum tunneling. This ultrasmall motor thus opens the possibility to investigatein operandoeffects and origins of energy dissipation during tunneling events, and, ultimately, energy harvesting at the atomic scales.

scholarly journals Molecular motors: forty years of interdisciplinary research

2011 ◽  
Vol 22 (21) ◽  
pp. 3936-3939 ◽  
Author(s):  
James A. Spudich
Keyword(s):  
Single Molecule ◽  
Molecular Motors ◽  
Atp Hydrolysis ◽  
Molecular Motor ◽  
Single Molecule Level ◽  
In Vitro Motility ◽  
Nonmuscle Cell ◽  
Nonmuscle Cells ◽  
City Plan

A mere forty years ago it was unclear what motor molecules exist in cells that could be responsible for the variety of nonmuscle cell movements, including the “saltatory cytoplasmic particle movements” apparent by light microscopy. One wondered whether nonmuscle cells might have a myosin-like molecule, well known to investigators of muscle. Now we know that there are more than a hundred different molecular motors in eukaryotic cells that drive numerous biological processes and organize the cell's dynamic city plan. Furthermore, in vitro motility assays, taken to the single-molecule level using techniques of physics, have allowed detailed characterization of the processes by which motor molecules transduce the chemical energy of ATP hydrolysis into mechanical movement. Molecular motor research is now at an exciting threshold of being able to enter into the realm of clinical applications.

scholarly journals Reconstitution of dynein transport to the microtubule plus end by kinesin

eLife ◽  
2014 ◽  
Vol 3 ◽  
Author(s):  
Anthony J Roberts ◽  
Brian S Goodman ◽  
Samara L Reck-Peterson
Keyword(s):  
Single Molecule ◽  
Molecular Motor ◽  
Cytoplasmic Dynein ◽  
Directed Motion ◽  
Microtubule Associated Proteins ◽  
Spatial Regulation ◽  
Intracellular Movement ◽  
Associated Proteins ◽  
Directed Motility ◽  
Dynamic Microtubule

Cytoplasmic dynein powers intracellular movement of cargo toward the microtubule minus end. The first step in a variety of dynein transport events is the targeting of dynein to the dynamic microtubule plus end, but the molecular mechanism underlying this spatial regulation is not understood. Here, we reconstitute dynein plus-end transport using purified proteins from S. cerevisiae and dissect the mechanism using single-molecule microscopy. We find that two proteins–homologs of Lis1 and Clip170–are sufficient to couple dynein to Kip2, a plus-end-directed kinesin. Dynein is transported to the plus end by Kip2, but is not a passive passenger, resisting its own plus-end-directed motion. Two microtubule-associated proteins, homologs of Clip170 and EB1, act as processivity factors for Kip2, helping it overcome dynein's intrinsic minus-end-directed motility. This reveals how a minimal system of proteins transports a molecular motor to the start of its track.

scholarly journals Single-molecule FRET dynamics of molecular motors in an ABEL Trap

2020 ◽  
Author(s):  
Maria Dienerowitz ◽  
Jamieson A. L. Howard ◽  
Steven D. Quinn ◽  
Frank Dienerowitz ◽  
Mark C. Leake
Keyword(s):  
Dna Replication ◽  
Single Molecule ◽  
Conformational Changes ◽  
Molecular Motors ◽  
Rational Design ◽  
Molecular Motor ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Observation Time

AbstractSingle-molecule Förster resonance energy transfer (smFRET) of molecular motors provides transformative insights into their dynamics and conformational changes both at high temporal and spatial resolution simultaneously. However, a key challenge of such FRET investigations is to observe a molecule in action for long enough without restricting its natural function. The Anti-Brownian ELectrokinetic Trap (ABEL trap) sets out to combine smFRET with molecular confinement to enable observation times of up to several seconds while removing any requirement of tethered surface attachment of the molecule in question. In addition, the ABEL trap’s inherent ability to selectively capture FRET active molecules accelerates the data acquisition process. Here we exemplify the capabilities of the ABEL trap in performing extended timescale smFRET measurements on the molecular motor Rep, which is crucial for removing protein blocks ahead of the advancing DNA replication machinery and for restarting stalled DNA replication. We are able to monitor single Rep molecules up to 6 s with 1 ms time resolution capturing multiple conformational switching events during the observation time. Here we provide a step-by-step guide for the rational design, construction and implementation of the ABEL trap for smFRET detection of Rep in vitro. We include details of how to model the electric potential at the trap site and use Hidden Markov analysis of the smFRET trajectories.

scholarly journals Temperature-Dependent Activity of Motor Proteins: Energetics and Their Implications for Collective Behavior

2021 ◽  
Vol 9 ◽  
Author(s):  
Saumya Yadav ◽  
Ambarish Kunwar
Keyword(s):  
Single Molecule ◽  
Molecular Motors ◽  
Intracellular Transport ◽  
Motor Proteins ◽  
Atp Hydrolysis ◽  
Molecular Motor ◽  
Surrounding Medium ◽  
Biochemical Properties ◽  
Cellular Transport ◽  
Temperature Dependent

Molecular motor proteins are an extremely important component of the cellular transport system that harness chemical energy derived from ATP hydrolysis to carry out directed mechanical motion inside the cells. Transport properties of these motors such as processivity, velocity, and their load dependence have been well established through single-molecule experiments. Temperature dependent biophysical properties of molecular motors are now being probed using single-molecule experiments. Additionally, the temperature dependent biochemical properties of motors (ATPase activity) are probed to understand the underlying mechanisms and their possible implications on the enzymatic activity of motor proteins. These experiments in turn have revealed their activation energies and how they compare with the thermal energy available from the surrounding medium. In this review, we summarize such temperature dependent biophysical and biochemical properties of linear and rotary motor proteins and their implications for collective function during intracellular transport and cellular movement, respectively.

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