Conventional theory predicts that molecular bond strength becomes trivial at very low loading rates, which, however, failed in some experiments probably due to hidden rebinding. Here we propose average bond strength as an alternative physical quantity to be measured in dynamic force spectroscopy experiments. Our analysis indicates that there exists an asymptotic value of average bond strength at low loading rates, which, nevertheless, increases with the spring constant of the loading system. This finding is subsequently confirmed with the Monte Carlo simulation. The proposed average bond strength can be informative in the understanding of the intriguing behaviors of molecular bonds at low loading rates
We probe the dynamic strength of multiple biotin-streptavidin adhesion bonds under linear loading us...
We use molecular dynamics to determine the force needed to rupture a chain molecule being stretched ...
<p>Loading rate dependence of the average unfolding force for the two most frequent transitions: Δ<i...
Existing experimental and theoretical studies on the adhesion of molecular bond clusters are usually...
In biology, molecular linkages at, within, and beneath cell interfaces arise mainly from weak noncov...
I develop an analytically tractable model of dynamic force spectroscopy by considering the forced es...
The dynamical strength of adhesion molecules under a time-dependent force is studied theoretically u...
AbstractSingle-molecule force spectroscopy is used to probe the kinetics of receptor-ligand bonds by...
We show that the standard theoretical framework in single-molecule force spectroscopy has to be exte...
AbstractIn dynamic force spectroscopy, a (bio-)molecular complex is subjected to a steadily increasi...
Getfert S, Reimann P. Hidden Multiple Bond Effects in Dynamic Force Spectroscopy. Biophysical Journa...
ABSTRACT We show that the standard theoretical framework in single-molecule force spectroscopy has t...
AbstractWe show that the standard theoretical framework in single-molecule force spectroscopy has to...
Atomic force microscope based single-molecule force spectroscopy provides a description of a variety...
A possible way to extract information about the reversible dissociation of a molecular adhe-sion bon...
We probe the dynamic strength of multiple biotin-streptavidin adhesion bonds under linear loading us...
We use molecular dynamics to determine the force needed to rupture a chain molecule being stretched ...
<p>Loading rate dependence of the average unfolding force for the two most frequent transitions: Δ<i...
Existing experimental and theoretical studies on the adhesion of molecular bond clusters are usually...
In biology, molecular linkages at, within, and beneath cell interfaces arise mainly from weak noncov...
I develop an analytically tractable model of dynamic force spectroscopy by considering the forced es...
The dynamical strength of adhesion molecules under a time-dependent force is studied theoretically u...
AbstractSingle-molecule force spectroscopy is used to probe the kinetics of receptor-ligand bonds by...
We show that the standard theoretical framework in single-molecule force spectroscopy has to be exte...
AbstractIn dynamic force spectroscopy, a (bio-)molecular complex is subjected to a steadily increasi...
Getfert S, Reimann P. Hidden Multiple Bond Effects in Dynamic Force Spectroscopy. Biophysical Journa...
ABSTRACT We show that the standard theoretical framework in single-molecule force spectroscopy has t...
AbstractWe show that the standard theoretical framework in single-molecule force spectroscopy has to...
Atomic force microscope based single-molecule force spectroscopy provides a description of a variety...
A possible way to extract information about the reversible dissociation of a molecular adhe-sion bon...
We probe the dynamic strength of multiple biotin-streptavidin adhesion bonds under linear loading us...
We use molecular dynamics to determine the force needed to rupture a chain molecule being stretched ...
<p>Loading rate dependence of the average unfolding force for the two most frequent transitions: Δ<i...