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.

journal_name

Nat Methods

journal_title

Nature methods

authors

Gambin Y,VanDelinder V,Ferreon AC,Lemke EA,Groisman A,Deniz AA

doi

10.1038/nmeth.1568

subject

Has Abstract

pub_date

2011-03-01 00:00:00

pages

239-41

issue

3

eissn

1548-7091

issn

1548-7105

pii

nmeth.1568

journal_volume

8

pub_type

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