Theoretical analysis of dynamic force spectroscopy experiments on ligand-receptor complexes

M. Raible; M. Evstigneev; P. Reimann; F. W. Bartels; R. Ros

doi:10.1016/j.jbiotec.2004.04.017

Theoretical analysis of dynamic force spectroscopy experiments on ligand-receptor complexes

M. Raible, M. Evstigneev, P. Reimann, F. W. Bartels, R. Ros

Research output: Contribution to journal › Article › peer-review

41 Scopus citations

Abstract

The forced rupture of single chemical bonds in biomolecular compounds (e.g. ligand-receptor systems) as observed in dynamic force spectroscopy experiments is addressed. Under the assumption that the probability of bond rupture depends only on the instantaneously acting force, a data collapse onto a single master curve is predicted. For rupture data obtained experimentally by dynamic AFM force spectroscopy of a ligand-receptor bond between a DNA and a regulatory protein we do not find such a collapse. We conclude that the above mentioned, generally accepted assumption is not satisfied and we discuss possible explanations.

Original language	English (US)
Pages (from-to)	13-23
Number of pages	11
Journal	Journal of Biotechnology
Volume	112
Issue number	1-2
DOIs	https://doi.org/10.1016/j.jbiotec.2004.04.017
State	Published - Aug 26 2004
Externally published	Yes

Keywords

Chemical reaction kinetics
Single molecule force spectroscopy

ASJC Scopus subject areas

Biotechnology
Bioengineering
Applied Microbiology and Biotechnology

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10.1016/j.jbiotec.2004.04.017

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title = "Theoretical analysis of dynamic force spectroscopy experiments on ligand-receptor complexes",

abstract = "The forced rupture of single chemical bonds in biomolecular compounds (e.g. ligand-receptor systems) as observed in dynamic force spectroscopy experiments is addressed. Under the assumption that the probability of bond rupture depends only on the instantaneously acting force, a data collapse onto a single master curve is predicted. For rupture data obtained experimentally by dynamic AFM force spectroscopy of a ligand-receptor bond between a DNA and a regulatory protein we do not find such a collapse. We conclude that the above mentioned, generally accepted assumption is not satisfied and we discuss possible explanations.",

keywords = "Chemical reaction kinetics, Single molecule force spectroscopy",

author = "M. Raible and M. Evstigneev and P. Reimann and Bartels, {F. W.} and R. Ros",

note = "Funding Information: Helpful discussions with R. Eckel, D. Anselmetti, R. Eichhorn, and especially R. Merkel are gratefully acknowledged. This work was supported by Deutsche Forschungsgemeinschaft under SFB 613 (Teilprojekt K7), the Alexander von Humboldt-Stiftung, and the ESF-program STOCHDYN.",

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doi = "10.1016/j.jbiotec.2004.04.017",

language = "English (US)",

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T1 - Theoretical analysis of dynamic force spectroscopy experiments on ligand-receptor complexes

AU - Raible, M.

AU - Evstigneev, M.

AU - Reimann, P.

AU - Bartels, F. W.

AU - Ros, R.

N1 - Funding Information: Helpful discussions with R. Eckel, D. Anselmetti, R. Eichhorn, and especially R. Merkel are gratefully acknowledged. This work was supported by Deutsche Forschungsgemeinschaft under SFB 613 (Teilprojekt K7), the Alexander von Humboldt-Stiftung, and the ESF-program STOCHDYN.

PY - 2004/8/26

Y1 - 2004/8/26

N2 - The forced rupture of single chemical bonds in biomolecular compounds (e.g. ligand-receptor systems) as observed in dynamic force spectroscopy experiments is addressed. Under the assumption that the probability of bond rupture depends only on the instantaneously acting force, a data collapse onto a single master curve is predicted. For rupture data obtained experimentally by dynamic AFM force spectroscopy of a ligand-receptor bond between a DNA and a regulatory protein we do not find such a collapse. We conclude that the above mentioned, generally accepted assumption is not satisfied and we discuss possible explanations.

AB - The forced rupture of single chemical bonds in biomolecular compounds (e.g. ligand-receptor systems) as observed in dynamic force spectroscopy experiments is addressed. Under the assumption that the probability of bond rupture depends only on the instantaneously acting force, a data collapse onto a single master curve is predicted. For rupture data obtained experimentally by dynamic AFM force spectroscopy of a ligand-receptor bond between a DNA and a regulatory protein we do not find such a collapse. We conclude that the above mentioned, generally accepted assumption is not satisfied and we discuss possible explanations.

KW - Chemical reaction kinetics

KW - Single molecule force spectroscopy

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DO - 10.1016/j.jbiotec.2004.04.017

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SP - 13

EP - 23

JO - Journal of Biotechnology

JF - Journal of Biotechnology

IS - 1-2

ER -

Theoretical analysis of dynamic force spectroscopy experiments on ligand-receptor complexes

Abstract

Keywords

ASJC Scopus subject areas

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