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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 ?-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.

SUBMITTER: Gambin Y

PROVIDER: S-EPMC3071799 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature

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Visualizing a one-way protein encounter complex by ultrafast single-molecule mixing.

Gambin Yann Y VanDelinder Virginia V Ferreon Allan Chris M AC Lemke Edward A EA Groisman Alex A Deniz Ashok A AA

Nature methods 20110206 3

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 ...[more]

PMID: 21297620

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