http://www.cnr.it/ontology/cnr/individuo/prodotto/ID175858
Force-clamp spectroscopy with a small dithering of AFM tip, and its application to explore the energy landscape of single avidin-biotin complex (Articolo in rivista)
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- Force-clamp spectroscopy with a small dithering of AFM tip, and its application to explore the energy landscape of single avidin-biotin complex (Articolo in rivista) (literal)
- Anno
- 2007-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.ultramic.2007.04.010 (literal)
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Melanie Favre (1); Lilia A. Chtcheglova (1); Dimitri A. Lapshin (2); Sergej K. Sekatskii (1); Francesco Valle (1); Giovanni Dietler (1) (2007)
Force-clamp spectroscopy with a small dithering of AFM tip, and its application to explore the energy landscape of single avidin-biotin complex
in Ultramicroscopy (Amst.); Elsevier, Amsterdam (Paesi Bassi)
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- Melanie Favre (1); Lilia A. Chtcheglova (1); Dimitri A. Lapshin (2); Sergej K. Sekatskii (1); Francesco Valle (1); Giovanni Dietler (1) (literal)
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- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- (1) Ecole Polytechnique Federale de Lausanne, LPMV (2) Russian Academy of Sciences (literal)
- Titolo
- Force-clamp spectroscopy with a small dithering of AFM tip, and its application to explore the energy landscape of single avidin-biotin complex (literal)
- Abstract
- We have recently developed a new method for directly measuring the spring constant of single molecules and molecular complexes on a real-time basis [L.A. Chtcheglova, G.T. Shubeita, S.K. Sekatskii, G. Dietler, Biophys. J. 86 (2004) 1177]. The technique combines standard force spectroscopy with a small dithering of tip. Changes in the amplitude of the oscillations are measured as a function of the pulling-off force to yield the spring constant of the complex. In this report, we present the first results of combination of this approach with the force-clamp spectroscopy. The standard atomic-force microscope has been supplemented with an electronic unit, which is capable of realizing an arbitrary force function, and permits the force-loading regime to be interrupted at any time. Using this method, 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. The energy landscape of the avidin-biotin complex is explored and discussed. (literal)
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