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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