Literature DB >> 18571862

Single-molecule avidin-biotin association reaction studied by force-clamp spectroscopy.

Mélanie Favre1, Serguei K Sekatskii, Giovanni Dietler.   

Abstract

Using single-molecule force-clamp spectroscopy, where the distance between the AFM tip and the sample surface is fixed and a few parallel avidin-biotin complexes are kept stretched by a certain force, we were able to observe the formation of single avidin-biotin bonds. Perspectives to use such an approach to study association reactions at single-molecule level in the conditions resembling those characteristic for some processes in vivo (e.g. virus-cell membrane attachment) are briefly discussed.

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Year:  2008        PMID: 18571862     DOI: 10.1016/j.ultramic.2008.04.058

Source DB:  PubMed          Journal:  Ultramicroscopy        ISSN: 0304-3991            Impact factor:   2.689


  2 in total

1.  Atomic force microscope based biomolecular force-clamp measurements using a micromachined electrostatic actuator.

Authors:  Hamdi Torun; Ofer Finkler; F Levent Degertekin
Journal:  Ultramicroscopy       Date:  2012-07-31       Impact factor: 2.689

2.  Mechanochemistry: one bond at a time.

Authors:  Jian Liang; Julio M Fernández
Journal:  ACS Nano       Date:  2009-07-02       Impact factor: 15.881

  2 in total

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