<p>(A) Force spectroscopy data obtained during the bond rupture between E1-5 constructs attached to a gold-coated AFM tip and a gold-covered glass slide (see scheme). A typical force extension curve shows the unbinding of E1-5 dimers in the absence of calcium ions (grey) and the presence of calcium ions (green). The extension curves show nonlinear stretching behavior preceding bond rupture. The rupture force histogram (green) reveals two major maxima potentially corresponding to two types of bonds. (B) Corresponding SMFS data of force-assisted unbinding of E1-2/E1-2 (red) or (C) E1-5/E1-2 (orange) cadherin molecules attached to tip and substrate as illustrated in the schemes. Tip substrate contact time was 0.1 s and pulling velocity was 1 μ...
International audienceThe mechanical properties of cells and of subcellular components are important...
AbstractIn dynamic force spectroscopy, a (bio-)molecular complex is subjected to a steadily increasi...
AbstractWe present the measurement of the force required to rupture a single protein-sugar bond usin...
Traditionally, adhesion interactions have been studied in reversible equilibrium conditions. Howeve...
Traditionally, adhesion interactions have been studied in reversible equilibrium conditions. Howeve...
The power of the Force: The rupture force of supramolecular bonds, as well as the unbinding dynamics...
The atomic force microscope (AFM) is able to manipulate biomolecules and their complexes with exquis...
Atomic force microscope based single-molecule force spectroscopy provides a description of a variety...
Dynamic force spectroscopy (DFS) makes it possible to investigate specific interactions between two ...
none1noTraditionally, adhesion interactions have been studied in reversible equilibrium conditions. ...
The atomic force microscope (AFM) is able to manipulate biomolecules and their complexes with exquis...
AbstractForce spectroscopy measurements of the rupture of the molecular bond between biotin and stre...
AFM-based dynamic single-molecule force spectroscopy was used to stretch carboxymethylated amylose (...
Many processes in the body are effected and regulated by highly, specialized protein molecules: Thes...
none1noTraditionally, protein-protein adhesion interactions have been studied in reversible equilibr...
International audienceThe mechanical properties of cells and of subcellular components are important...
AbstractIn dynamic force spectroscopy, a (bio-)molecular complex is subjected to a steadily increasi...
AbstractWe present the measurement of the force required to rupture a single protein-sugar bond usin...
Traditionally, adhesion interactions have been studied in reversible equilibrium conditions. Howeve...
Traditionally, adhesion interactions have been studied in reversible equilibrium conditions. Howeve...
The power of the Force: The rupture force of supramolecular bonds, as well as the unbinding dynamics...
The atomic force microscope (AFM) is able to manipulate biomolecules and their complexes with exquis...
Atomic force microscope based single-molecule force spectroscopy provides a description of a variety...
Dynamic force spectroscopy (DFS) makes it possible to investigate specific interactions between two ...
none1noTraditionally, adhesion interactions have been studied in reversible equilibrium conditions. ...
The atomic force microscope (AFM) is able to manipulate biomolecules and their complexes with exquis...
AbstractForce spectroscopy measurements of the rupture of the molecular bond between biotin and stre...
AFM-based dynamic single-molecule force spectroscopy was used to stretch carboxymethylated amylose (...
Many processes in the body are effected and regulated by highly, specialized protein molecules: Thes...
none1noTraditionally, protein-protein adhesion interactions have been studied in reversible equilibr...
International audienceThe mechanical properties of cells and of subcellular components are important...
AbstractIn dynamic force spectroscopy, a (bio-)molecular complex is subjected to a steadily increasi...
AbstractWe present the measurement of the force required to rupture a single protein-sugar bond usin...