The Kinetics of Chemical Reactions: Single-Molecule Versus “Bulk” View

2015 ◽  
pp. 29-38
Keyword(s):  
Chemical Reactions ◽  
Single Molecule ◽  
Kinetics Of

New highly efficient coulometric cell with homogenous potential distribution on the working electrode

1986 ◽  
Vol 51 (3) ◽  
pp. 636-642
Author(s):  
Michal Németh ◽  
Ján Mocák
Keyword(s):  
Chemical Reactions ◽  
Potential Distribution ◽  
Anaerobic Conditions ◽  
Highly Efficient ◽  
Working Electrode ◽  
Constant Potential ◽  
Quantitative Analyses ◽  
Mechanism And Kinetics ◽  
Kinetics Of

A highly efficient coulometric cell was designed and constructed, ensuring a constant potential over the whole surface of the working electrode and suitable for very rapid electrolysis. It consists of concentric cylindrical Teflon parts; also the working and auxiliary electrodes are cylindrical and concentric. Electrolysis can be carried out under anaerobic conditions. Functioning of the cell was tested on the oxidation of hexacyanoferrate(II) and chlorpromazine and reduction of hexacyanoferrate(III). The new cell is suitable for routine quantitative analyses and in studying the mechanism and kinetics of moderately rapid chemical reactions.

Single-Molecule Force-Clamp Experiments Reveal Kinetics of Mechanically Activated Silyl Ester Hydrolysis

ACS Nano ◽  
2012 ◽  
Vol 6 (2) ◽  
pp. 1314-1321 ◽  
Author(s):  
Sebastian W. Schmidt ◽  
Pavel Filippov ◽  
Alfred Kersch ◽  
Martin K. Beyer ◽  
Hauke Clausen-Schaumann
Keyword(s):  
Single Molecule ◽  
Ester Hydrolysis ◽  
Silyl Ester ◽  
Force Clamp ◽  
Kinetics Of

scholarly journals Increasing the time resolution of single-molecule experiments with Bayesian inference

2017 ◽  
Author(s):  
Colin D. Kinz-Thompson ◽  
Ruben L. Gonzalez
Keyword(s):  
Bayesian Inference ◽  
Single Molecule ◽  
Time Resolution ◽  
Rate Constants ◽  
Computational Approach ◽  
Biomolecular Systems ◽  
Time Resolved ◽  
The Given ◽  
Kinetics Of ◽  
Resolution Data

AbstractMany time-resolved, single-molecule biophysics experiments seek to characterize the kinetics of biomolecular systems exhibiting dynamics that challenge the time resolution of the given technique. Here we present a general, computational approach to this problem that employs Bayesian inference to learn the underlying dynamics of such systems, even when they are much faster than the time resolution of the experimental technique being used. By accurately and precisely inferring rate constants, our Bayesian Inference for the Analysis of Sub-temporal-resolution Data (BIASD) approach effectively enables the experimenter to super-resolve the poorly resolved dynamics that are present in their data.

scholarly journals Dynamics of Tpm1.8 domains on actin filaments with single molecule resolution

2020 ◽  
Author(s):  
Ilina Bareja ◽  
Hugo Wioland ◽  
Miro Janco ◽  
Philip R. Nicovich ◽  
Antoine Jégou ◽  
...  
Keyword(s):  
Actin Filament ◽  
Single Molecule ◽  
Actin Filaments ◽  
High Probability ◽  
Actin Binding ◽  
Single Molecule Level ◽  
Filament Dynamics ◽  
Kinetics Of ◽  
Insight Into

ABSTRACTTropomyosins regulate dynamics and functions of the actin cytoskeleton by forming long chains along the two strands of actin filaments that act as gatekeepers for the binding of other actin-binding proteins. The fundamental molecular interactions underlying the binding of tropomyosin to actin are still poorly understood. Using microfluidics and fluorescence microscopy, we observed the binding of fluorescently labelled tropomyosin isoform Tpm1.8 to unlabelled actin filaments in real time. This approach in conjunction with mathematical modeling enabled us to quantify the nucleation, assembly and disassembly kinetics of Tpm1.8 on single filaments and at the single molecule level. Our analysis suggests that Tpm1.8 decorates the two strands of the actin filament independently. Nucleation of a growing tropomyosin domain proceeds with high probability as soon as the first Tpm1.8 molecule is stabilised by the addition of a second molecule, ultimately leading to full decoration of the actin filament. In addition, Tpm1.8 domains are asymmetrical, with enhanced dynamics at the edge oriented towards the barbed end of the actin filament. The complete description of Tpm1.8 kinetics on actin filaments presented here provides molecular insight into actin-tropomyosin filament formation and the role of tropomyosins in regulating actin filament dynamics.

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