Force-clamp spectroscopy with a small dithering of AFM tip, and its application to explore the energy landscape of single avidin-biotin complex.
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Summary
The first results of combination of this approach with the force-clamp spectroscopy are presented, which shows the time needed to rupture a single bond can be measured as a function of the force that is required to maintain the complex in a stretched condition.
- Type
- article
- Published
- 2007-10-01
- Cited by
- 10
- References
- 27
- OpenAlex
- https://openalex.org/W17560032
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:31635678
Keywords
Computer science
References
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- Ligand Binding: Molecular Mechanics Calculation of the Streptavidin-Biotin Rupture Force
- Temperature Dependence of the Biotin−Avidin Bond-Rupture Force Studied by Atomic Force Microscopy
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- Optimal sensitivity for molecular recognition MAC-mode AFM
- Energy landscapes of receptor–ligand bonds explored with dynamic force spectroscopy
- Dynamic force measurements of avidin-biotin and streptavdin-biotin interactions using AFM.
- Relationship between Stiffness and Force in Single Molecule Pulling Experiments
- Models for the specific adhesion of cells to cells.
- Dynamic force spectroscopy of molecular adhesion bonds.
- Molecular force modulation spectroscopy revealing the dynamic response of single bacteriorhodopsins.
- Loading-rate dependence of individual ligand-receptor bond-rupture forces studied by atomic force microscopy
- Force-Clamp Spectroscopy Monitors the Folding Trajectory of a Single Protein
- Chemically distinct transition states govern rapid dissociation of single L-selectin bonds under force
- Beyond the conventional description of dynamic force spectroscopy of adhesion bonds
Cited by
- Characterization of glycoprotein E C-End of West Nile virus and evaluation of its interaction force with αVβ3 integrin as putative cellular receptor
- Dependence of the most probable and average bond rupture force on the force loading rate: First order correction to the Bell–Evans model
- Single-molecule avidin-biotin association reaction studied by force-clamp spectroscopy.
- Pathogenic Mutations Shift the Equilibria of α‐Synuclein Single Molecules towards Structured Conformers
- Force dependency of biochemical reactions measured by single molecule force-clamp spectroscopy
- Statistical Study of the Unfolding of Multimodular Proteins and their Energy Landscape by Atomic Force Microscopy
- Ideal, catch, and slip bonds in cadherin adhesion
- Force spectroscopy of barnase–barstar single molecule interaction
- Can Dissipative Properties of Single Molecules Be Extracted from a Force Spectroscopy Experiment?
- Double-peak resonant mapping of cellular viscoelasticity in force-clamp detection of atomic force microscope
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