Towards Powering Nanometer-Scale Devices with Molecular Motors: Single Molecule Engines

2006 ◽  
Vol 207 (6) ◽  
pp. 573-575 ◽  
Author(s):  
Hans-Jürgen Butt
Keyword(s):  
Single Molecule ◽  
Molecular Motors ◽  
Nanometer Scale

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.

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

Methods ◽  
2021 ◽  
Author(s):  
Maria Dienerowitz ◽  
Jamieson A.L. Howard ◽  
Steven D. Quinn ◽  
Frank Dienerowitz ◽  
Mark C. Leake
Keyword(s):  
Single Molecule ◽  
Molecular Motors ◽  
Single Molecule Fret

Single Molecule Height Measurements on a Membrane Protein in Nanometer-Scale Phospholipid Bilayer Disks

Langmuir ◽  
2000 ◽  
Vol 16 (14) ◽  
pp. 5993-5997 ◽  
Author(s):  
Timothy H. Bayburt ◽  
Joseph W. Carlson ◽  
Stephen G. Sligar
Keyword(s):  
Membrane Protein ◽  
Single Molecule ◽  
Phospholipid Bilayer ◽  
Nanometer Scale

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.

scholarly journals Stochastically pumped adaptation and directional motion of molecular machines

2018 ◽  
Vol 115 (38) ◽  
pp. 9405-9413 ◽  
Author(s):  
R. Dean Astumian
Keyword(s):  
Single Molecule ◽  
Molecular Motors ◽  
High Efficiency ◽  
Probability Distributions ◽  
Molecular Machines ◽  
High Energy ◽  
Stochastic Thermodynamics ◽  
Recent Developments ◽  
Directional Motion ◽  
External Fluctuations

Recent developments in synthetic molecular motors and pumps have sprung from a remarkable confluence of experiment and theory. Synthetic accomplishments have facilitated the ability to design and create molecules, many of them featuring mechanically bonded components, to carry out specific functions in their environment—walking along a polymeric track, unidirectional circling of one ring about another, synthesizing stereoisomers according to an external protocol, or pumping rings onto a long rod-like molecule to form and maintain high-energy, complex, nonequilibrium structures from simpler antecedents. Progress in the theory of nanoscale stochastic thermodynamics, specifically the generalization and extension of the principle of microscopic reversibility to the single-molecule regime, has enhanced the understanding of the design requirements for achieving strong unidirectional motion and high efficiency of these synthetic molecular machines for harnessing energy from external fluctuations to carry out mechanical and/or chemical functions in their environment. A key insight is that the interaction between the fluctuations and the transition state energies plays a central role in determining the steady-state concentrations. Kinetic asymmetry, a requirement for stochastic adaptation, occurs when there is an imbalance in the effect of the fluctuations on the forward and reverse rate constants. Because of strong viscosity, the motions of the machine can be viewed as mechanical equilibrium processes where mechanical resonances are simply impossible but where the probability distributions for the state occupancies and trajectories are very different from those that would be expected at thermodynamic equilibrium.

scholarly journals Cost-efficient nanoscopy reveals nanoscale architecture of liver cells and platelets

Nanophotonics ◽  
2019 ◽  
Vol 8 (7) ◽  
pp. 1299-1313 ◽  
Author(s):  
Hong Mao ◽  
Robin Diekmann ◽  
Hai Po H. Liang ◽  
Victoria C. Cogger ◽  
David G. Le Couteur ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Endothelial Cells ◽  
Single Molecule ◽  
Nanometer Scale ◽  
Color Channel ◽  
Liver Sinusoidal Endothelial Cells ◽  
Localization Microscopy ◽  
Cost Efficient ◽  
Core Facilities ◽  
Single Molecule Localization Microscopy

AbstractSingle-molecule localization microscopy (SMLM) provides a powerful toolkit to specifically resolve intracellular structures on the nanometer scale, even approaching resolution classically reserved for electron microscopy (EM). Although instruments for SMLM are technically simple to implement, researchers tend to stick to commercial microscopes for SMLM implementations. Here we report the construction and use of a “custom-built” multi-color channel SMLM system to study liver sinusoidal endothelial cells (LSECs) and platelets, which costs significantly less than a commercial system. This microscope allows the introduction of highly affordable and low-maintenance SMLM hardware and methods to laboratories that, for example, lack access to core facilities housing high-end commercial microscopes for SMLM and EM. Using our custom-built microscope and freely available software from image acquisition to analysis, we image LSECs and platelets with lateral resolution down to about 50 nm. Furthermore, we use this microscope to examine the effect of drugs and toxins on cellular morphology.

[12] Molecular motors and single-molecule enzymology

2003 ◽  
pp. 228-245 ◽  
Author(s):  
Yoshiharu Ishii ◽  
Kazuo Kitamura ◽  
Hiroto Tanaka ◽  
Toshio Yanagida
Keyword(s):  
Single Molecule ◽  
Molecular Motors ◽  
Single Molecule Enzymology

scholarly journals A Generalized Kinetic Model for Coupling between Stepping and ATP Hydrolysis of Kinesin Molecular Motors

2019 ◽  
Vol 20 (19) ◽  
pp. 4911 ◽  
Author(s):  
Xie ◽  
Guo ◽  
Chen
Keyword(s):  
Kinetic Model ◽  
Atpase Activity ◽  
Single Molecule ◽  
Rate Constants ◽  
Molecular Motors ◽  
Atp Hydrolysis ◽  
Power Production ◽  
Wild Type ◽  
Chemomechanical Coupling ◽  
Generalized Kinetic Model

A general kinetic model is presented for the chemomechanical coupling of dimeric kinesin molecular motors with and without extension of their neck linkers (NLs). A peculiar feature of the model is that the rate constants of ATPase activity of a kinesin head are independent of the strain on its NL, implying that the heads of the wild-type kinesin dimer and the mutant with extension of its NLs have the same force-independent rate constants of the ATPase activity. Based on the model, an analytical theory is presented on the force dependence of the dynamics of kinesin dimers with and without extension of their NLs at saturating ATP. With only a few adjustable parameters, diverse available single molecule data on the dynamics of various kinesin dimers, such as wild-type kinesin-1, kinesin-1 with mutated residues in the NLs, kinesin-1 with extension of the NLs and wild-type kinesin-2, under varying force and ATP concentration, can be reproduced very well. Additionally, we compare the power production among different kinesin dimers, showing that the mutation in the NLs reduces the power production and the extension of the NLs further reduces the power production.

Sign in / Sign up

Export Citation Format

Share Document