ArticleBiophysical journal2005
Multiple-bond kinetics from single-molecule pulling experiments: evidence for multiple NCAM bonds.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 34 citations in OpenAlex.
- Functionalization of AFM Tips and Supports for Molecular Recognition Force Spectroscopy and Recognition Imaging.Methods in molecular biology (Clifton, N.J.) · 2027Article
- Size-Dependent Affinity of Glycine and Its Short Oligomers to Pyrite Surface: A Model for Prebiotic Accumulation of Amino Acid Oligomers on a Mineral Surface.International journal of molecular sciences · 2018Article
- Atomic force microscopy measurements reveal multiple bonds between Helicobacter pylori blood group antigen binding adhesin and Lewis b ligand.Journal of the Royal Society, Interface · 2014Article
- Magnetic tweezers-based force clamp reveals mechanically distinct apCAM domain interactions.Biophysical journal · 2012Article
- Rupture of multiple receptor-ligand bonds: bimodal distribution of bond rupture force.The European physical journal. E, Soft matter · 2012Article
- Single-molecule force spectroscopy of the Aplysia cell adhesion molecule reveals two homophilic bonds.Biophysical journal · 2012Article
- A theoretical method to determine unstressed off-rate from multiple bond force spectroscopy.Colloids and surfaces. B, Biointerfaces · 2012Article
- Linking of sensor molecules with amino groups to amino-functionalized AFM tips.Bioconjugate chemistry · 2011Article
- Allosteric cross talk between cadherin extracellular domains.Biophysical journal · 2010Article
- Biophysical properties of cadherin bonds do not predict cell sorting.The Journal of biological chemistry · 2008Article
- Effects of multiple-bond ruptures on kinetic parameters extracted from force spectroscopy measurements: revisiting biotin-streptavidin interactions.Biophysical journal · 2008Article
- Exploring transferrin-receptor interactions at the single-molecule level.Biophysical journal · 2008Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The kinetic parameters of single bonds between neural cell adhesion molecules were determined from atomic force microscope measurements of the forced dissociation of the homophilic protein-protein bonds. The analytical approach described provides a systematic procedure for obtaining rupture kinetics for single protein bonds from bond breakage frequency distributions obtained from single-molecule pulling experiments. For these studies, we used the neural cell adhesion molecule (NCAM), which was recently shown to form two independent protein bonds. The analysis of the bond rupture data at different loading rates, using the single-bond full microscopic model, indicates that the breakage frequency distribution is most sensitive to the distance to the transition state and least sensitive to the molecular spring constant. The analysis of bond failure data, however, motivates the use of a double-bond microscopic model that requires an additional kinetic parameter. This double-bond microscopic model assumes two independent NCAM-NCAM bonds, and more accurately describes the breakage frequency distribution, particularly at high loading rates. This finding agrees with recent surface-force measurements, which showed that NCAM forms two spatially distinct bonds between opposed proteins.
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Registered trials
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