title: In situ monitoring of single molecule binding reactions with time-lapse atomic force microscopy on functionalized DNA origami.
abstract: Individual biomolecular binding events were recorded in situ by combining time-lapse atomic force microscopy and DNA origami. Single streptavidin molecules bound to specifically biotinyated DNA origami were simply counted as a function of time to obtain a direct measure of the binding rate.
authors.affiliation: Laboratory of Physical Biology, Shanghai Institute of Applied Physics, Chinese Academy of Sciences, Shanghai, 201800, China.
authors.forename: Na
authors.initials: N
authors.lastname: Wu
authors.forename: Xingfei
authors.initials: X
authors.lastname: Zhou
authors.forename: Daniel M
authors.initials: DM
authors.lastname: Czajkowsky
authors.forename: Ming
authors.initials: M
authors.lastname: Ye
authors.forename: Dongdong
authors.initials: D
authors.lastname: Zeng
authors.forename: Yanming
authors.initials: Y
authors.lastname: Fu
authors.forename: Chunhai
authors.initials: C
authors.lastname: Fan
authors.forename: Jun
authors.initials: J
authors.lastname: Hu
authors.forename: Bin
authors.initials: B
authors.lastname: Li
mesh_terms: D001710:Biotin / Q000737:chemistry / Q000378:metabolism; D004247:DNA / Q000737:chemistry*; D018625:Microscopy, Atomic Force / Q000379:methods*; D036103:Nanotechnology / Q000379:methods*; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D019809:Streptavidin / Q000737:chemistry / Q000378:metabolism; D059008:Time-Lapse Imaging / Q000379:methods*
chemical_list: D001710:Biotin; D004247:DNA; D019809:Streptavidin