Journal
NATURE METHODS
Volume 8, Issue 3, Pages 239-U77Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/NMETH.1568
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Funding
- US National Institutes of Health [RO1 GM066833, R21 AG033382]
- National Science Foundation [PHY-0750049]
- Deutsche Forschungsgemeinschaft
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We combined rapid microfluidic mixing with single-molecule fluorescence resonance energy transfer to study the folding kinetics of the intrinsically disordered human protein alpha-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.
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