title: Visualizing a one-way protein encounter complex by ultrafast single-molecule mixing.
abstract: We combined rapid microfluidic mixing with single-molecule fluorescence resonance energy transfer to study the folding kinetics of the intrinsically disordered human protein α-synuclein. The time-resolution of 0.2 ms revealed initial collapse of the unfolded protein induced by binding with lipid mimics and subsequent rapid formation of transient structures in the encounter complex. The method also enabled analysis of rapid dissociation and unfolding of weakly bound complexes triggered by massive dilution.
authors.affiliation: Department of Molecular Biology, The Scripps Research Institute, La Jolla, California, USA. y.gambin@imb.uq.edu
authors.forename: Yann
authors.initials: Y
authors.lastname: Gambin
authors.forename: Virginia
authors.initials: V
authors.lastname: VanDelinder
authors.forename: Allan Chris M
authors.initials: AC
authors.lastname: Ferreon
authors.forename: Edward A
authors.initials: EA
authors.lastname: Lemke
authors.forename: Alex
authors.initials: A
authors.lastname: Groisman
authors.forename: Ashok A
authors.initials: AA
authors.lastname: Deniz
mesh_terms: D031541:Fluorescence Resonance Energy Transfer / Q000379:methods*; D006801:Humans; D007700:Kinetics; D046210:Microfluidic Analytical Techniques / Q000379:methods*; D011485:Protein Binding; D017510:Protein Folding; D051844:alpha-Synuclein / Q000737:chemistry*
chemical_list: D051844:alpha-Synuclein