Visualizing a one-way protein encounter complex by ultrafast single-molecule mixing.
Nat Methods
; 8(3): 239-41, 2011 Mar.
Article
em En
| MEDLINE
| ID: mdl-21297620
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.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Transferência Ressonante de Energia de Fluorescência
/
Técnicas Analíticas Microfluídicas
/
Alfa-Sinucleína
Limite:
Humans
Idioma:
En
Ano de publicação:
2011
Tipo de documento:
Article