MétaCan
← all works

Probing the Relation Between Force—Lifetime—and Chemistry in Single Molecular Bonds

2001· review· en· 1,330 citations· W2125813323 on OpenAlex· 10.1146/annurev.biophys.30.1.105

Why is this work in the frame?

A frame that forgets how it found something cannot be audited. These are the routes that admitted this work.

Canadian affiliationAn author listed a Canadian institution. This is the only route the usual frame has.
Canadian funderA Canadian agency funded it. The work may carry no Canadian affiliation at all.

Machine scores (provisional)

Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.

The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.

Opus teacher head0.008
GPT teacher head0.292
Teacher spread
0.284 · how far apart the two teachers sit on this one work
Validation status
score_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from it

Abstract

On laboratory time scales, the energy landscape of a weak bond along a dissociation pathway is fully explored through Brownian-thermal excitations, and energy barriers become encoded in a dissociation time that varies with applied force. Probed with ramps of force over an enormous range of rates (force/time), this kinetic profile is transformed into a dynamic spectrum of bond rupture force as a function of loading rate. On a logarithmic scale in loading rate, the force spectrum provides an easy-to-read map of the prominent energy barriers traversed along the force-driven pathway and exposes the differences in energy between barriers. In this way, the method of dynamic force spectroscopy (DFS) is being used to probe the complex relation between force-lifetime-and chemistry in single molecular bonds. Most important, DFS probes the inner world of molecular interactions to reveal barriers that are difficult or impossible to detect in assays of near equilibrium dissociation but that determine bond lifetime and strength under rapid detachment. To use an ultrasensitive force probe as a spectroscopic tool, we need to understand the physics of bond dissociation under force, the impact of experimental technique on the measurement of detachment force (bond strength), the consequences of complex interactions in macromolecular bonds, and effects of multiply-bonded attachments.

Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.

The record

Venue
Annual Review of Biophysics and Biomolecular Structure
Topic
Force Microscopy Techniques and Applications
Field
Physics and Astronomy
Canadian institutions
University of British Columbia
Funders
National Heart, Lung, and Blood InstituteNational Institutes of HealthNational Health and Medical Research CouncilNational Medical Research CouncilMedical Research Council CanadaInstitut National de la Santé et de la Recherche MédicaleNational Institute for Health and Care Research
Keywords
Force spectroscopyDissociation (chemistry)Kinetic energyChemical physicsChemistryBond-dissociation energyBond strengthBond energyBond orderEnergy landscapeChemical bondSingle bondNanotechnologyBond lengthMoleculeMaterials sciencePhysical chemistryAtomic force microscopyPhysicsClassical mechanicsAdhesive
Has abstract in OpenAlex
yes