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 Methodsjournal_title
Nature methodsauthors
Gambin Y,VanDelinder V,Ferreon AC,Lemke EA,Groisman A,Deniz AAdoi
10.1038/nmeth.1568subject
Has Abstractpub_date
2011-03-01 00:00:00pages
239-41issue
3eissn
1548-7091issn
1548-7105pii
nmeth.1568journal_volume
8pub_type
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