Favre, MelanieSekatskii, Serguei K.Dietler, Giovanni2010-02-092010-02-092010-02-09200810.1016/j.ultramic.2008.04.058https://infoscience.epfl.ch/handle/20.500.14299/46516WOS:000259728000030Using 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 all 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. (C) 2008 Elsevier B.V. All rights reserved.force-clamp AFMsingle-molecule force spectroscopychemical bondsSERUM-ALBUMINENERGY LANDSCAPEAFM TIPMICROSCOPYPROTEINCOMPLEXESSTREPTAVIDINDEPENDENCEADHESIONBONDStext::conference output::conference proceedings::conference paper