Transverse Dynamic Force Spectroscopy:  A Novel Approach to Determining the Complex Stiffness of a Single Molecule

Langmuir ◽  
2002 ◽  
Vol 18 (5) ◽  
pp. 1729-1733 ◽  
Author(s):  
A. D. L. Humphris ◽  
M. Antognozzi ◽  
T. J. McMaster ◽  
M. J. Miles
Keyword(s):  
Single Molecule ◽  
Force Spectroscopy ◽  
Dynamic Force ◽  
Dynamic Force Spectroscopy ◽  
Transverse Dynamic ◽  
Novel Approach

Dynamic force spectroscopy for quantifying single-molecule organo–mineral interactions

CrystEngComm ◽  
2021 ◽  
Vol 23 (1) ◽  
pp. 11-23
Author(s):  
Hang Zhai ◽  
Wenjun Zhang ◽  
Lijun Wang ◽  
Christine V. Putnis
Keyword(s):  
Single Molecule ◽  
Force Spectroscopy ◽  
Nucleation And Growth ◽  
Crystal Nucleation ◽  
Dynamic Force ◽  
Dynamic Force Spectroscopy ◽  
Crystal Phases

Organo–mineral interactions have long been the focus in the fields of biomineralization and geomineralization, since such interactions not only modulate the dynamics of crystal nucleation and growth but may also change crystal phases, morphologies, and structures.

Interpretations of Receptor–Ligand Dissociation Kinetics from Single-Molecule Pulling Experiments

2017 ◽  
Vol 09 (03) ◽  
pp. 1750042 ◽  
Author(s):  
Yuan Feng ◽  
Ji Lin ◽  
Jin Qian
Keyword(s):  
Single Molecule ◽  
Gaussian Approximation ◽  
Force Spectroscopy ◽  
Thermal Fluctuations ◽  
Theoretical Issue ◽  
Dynamic Force ◽  
Dynamic Force Spectroscopy ◽  
Receptor Ligand ◽  
Bond Dissociation ◽  
Force Relation

The kinetic response of receptor–ligand bonds to externally imposed force is of essential importance for adhesion-mediated behaviors of cells. Two prevailing experimental approaches, so-called dynamic force spectroscopy and force clamp assay, have been commonly adopted to probe the force dependence of bond dissociation rate at single-molecule level. This study focuses on the outstanding theoretical issue concerning the distinct loading paths and different procedures to extract the kinetic information in the two types of experiments. To address the issue, Monte Carlo simulations have been performed to simulate bond dissociation as a well-to-barrier escape process under dynamically imposed force as well as thermal fluctuations, and the consistency of quantitative interpretations on force-dependent bond lifetimes from the different approaches is examined. Our numerical results show that all the interpretations from different methods collapse into a single master curve of lifetime–force relation for receptor–ligand bonds with slip behavior. However, for bonds with biphasic catch–slip behavior, a procedure based on a Gaussian approximation of rupture force distributions, proposed by Dudko for dynamic force spectroscopy, tends to underestimate bond lifetime for certain force range.

How does the molecular linker in dynamic force spectroscopy affect probing molecular interactions at the single-molecule level?

2016 ◽  
Vol 55 (8S1) ◽  
pp. 08NB01 ◽  
Author(s):  
Atsushi Taninaka ◽  
Kota Aizawa ◽  
Tatsuya Hanyu ◽  
Yuuichi Hirano ◽  
Osamu Takeuchi ◽  
...  
Keyword(s):  
Single Molecule ◽  
Molecular Interactions ◽  
Force Spectroscopy ◽  
Dynamic Force ◽  
Dynamic Force Spectroscopy ◽  
Single Molecule Level

Single-Molecule Study ofG-Quadruplex Disruption Using Dynamic Force Spectroscopy

2012 ◽  
Vol 109 (5) ◽  
Author(s):  
Michel de Messieres ◽  
Jen-Chien Chang ◽  
Barbara Brawn-Cinani ◽  
Arthur La Porta
Keyword(s):  
Single Molecule ◽  
Force Spectroscopy ◽  
Dynamic Force ◽  
Dynamic Force Spectroscopy

scholarly journals Dynamic force spectroscopy of synthetic oligorotaxane foldamers

2017 ◽  
Vol 115 (38) ◽  
pp. 9362-9366 ◽  
Author(s):  
Damien Sluysmans ◽  
Floriane Devaux ◽  
Carson J. Bruns ◽  
J. Fraser Stoddart ◽  
Anne-Sophie Duwez
Keyword(s):  
Single Molecule ◽  
Force Spectroscopy ◽  
Energy Difference ◽  
Dynamic Force ◽  
Kinetic Regime ◽  
Dynamic Force Spectroscopy ◽  
Loading Rates ◽  
Folded Structure ◽  
Donor Acceptor ◽  
Local Conformations

Wholly synthetic molecules involving both mechanical bonds and a folded secondary structure are one of the most promising architectures for the design of functional molecular machines with unprecedented properties. Here, we report dynamic single-molecule force spectroscopy experiments that explore the energetic details of donor–acceptor oligorotaxane foldamers, a class of molecular switches. The mechanical breaking of the donor–acceptor interactions responsible for the folded structure shows a high constant rupture force over a broad range of loading rates, covering three orders of magnitude. In comparison with dynamic force spectroscopy performed during the past 20 y on various (bio)molecules, the near-equilibrium regime of oligorotaxanes persists at much higher loading rates, at which biomolecules have reached their kinetic regime, illustrating the very fast dynamics and remarkable rebinding capabilities of the intramolecular donor–acceptor interactions. We focused on one single interaction at a time and probed the stochastic rupture and rebinding paths. Using the Crooks fluctuation theorem, we measured the mechanical work produced during the breaking and rebinding to determine a free-energy difference, ΔG, of 6 kcal·mol−1 between the two local conformations around a single bond.

Single-molecule dynamic force spectroscopy of the fibronectin–heparin interaction

2007 ◽  
Vol 364 (3) ◽  
pp. 595-600 ◽  
Author(s):  
Gabriel Mitchell ◽  
Charles-Antoine Lamontagne ◽  
Réjean Lebel ◽  
Michel Grandbois ◽  
François Malouin
Keyword(s):  
Single Molecule ◽  
Force Spectroscopy ◽  
Dynamic Force ◽  
Dynamic Force Spectroscopy ◽  
Heparin Interaction

Dynamic force spectroscopy of a single condensed DNA

2007 ◽  
Vol 79 (5) ◽  
pp. 58001 ◽  
Author(s):  
Y Murayama ◽  
H Wada ◽  
M Sano
Keyword(s):  
Force Spectroscopy ◽  
Dynamic Force ◽  
Dynamic Force Spectroscopy ◽  
Condensed Dna

scholarly journals Dissecting the cytochrome c2–reaction centre interaction in bacterial photosynthesis using single molecule force spectroscopy

2019 ◽  
Vol 476 (15) ◽  
pp. 2173-2190
Author(s):  
Cvetelin Vasilev ◽  
Guy E. Mayneord ◽  
Amanda A. Brindley ◽  
Matthew P. Johnson ◽  
C. Neil Hunter
Keyword(s):  
Single Molecule ◽  
Silicon Oxide ◽  
Fluorescent Protein ◽  
Dissociation Constants ◽  
Force Spectroscopy ◽  
Spectroscopic Studies ◽  
Bacterial Photosynthesis ◽  
Dynamic Force ◽  
Reaction Centre ◽  
Cytochrome C2

Abstract The reversible docking of small, diffusible redox proteins onto a membrane protein complex is a common feature of bacterial, mitochondrial and photosynthetic electron transfer (ET) chains. Spectroscopic studies of ensembles of such redox partners have been used to determine ET rates and dissociation constants. Here, we report a single-molecule analysis of the forces that stabilise transient ET complexes. We examined the interaction of two components of bacterial photosynthesis, cytochrome c2 and the reaction centre (RC) complex, using dynamic force spectroscopy and PeakForce quantitative nanomechanical imaging. RC–LH1–PufX complexes, attached to silicon nitride AFM probes and maintained in a photo-oxidised state, were lowered onto a silicon oxide substrate bearing dispersed, immobilised and reduced cytochrome c2 molecules. Microscale patterns of cytochrome c2 and the cyan fluorescent protein were used to validate the specificity of recognition between tip-attached RCs and surface-tethered cytochrome c2. Following the transient association of photo-oxidised RC and reduced cytochrome c2 molecules, retraction of the RC-functionalised probe met with resistance, and forces between 112 and 887 pN were required to disrupt the post-ET RC–c2 complex, depending on the retraction velocities used. If tip-attached RCs were reduced instead, the probability of interaction with reduced cytochrome c2 molecules decreased 5-fold. Thus, the redox states of the cytochrome c2 haem cofactor and RC ‘special pair’ bacteriochlorophyll dimer are important for establishing a productive ET complex. The millisecond persistence of the post-ET cytochrome c2[oxidised]–RC[reduced] ‘product’ state is compatible with rates of cyclic photosynthetic ET, at physiologically relevant light intensities.

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