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

We combined rapid microfluidic mixing with single-molecule Förster 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 a...

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Autores principales: Gambin, Yann, Vandelinder, Virginia, Ferreon, Allan Chris M., Lemke, Edward A., Groisman, Alex, Deniz, Ashok A.
Formato: Texto
Lenguaje:English
Publicado: 2011
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3071799/
https://www.ncbi.nlm.nih.gov/pubmed/21297620
http://dx.doi.org/10.1038/nmeth.1568
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author Gambin, Yann
Vandelinder, Virginia
Ferreon, Allan Chris M.
Lemke, Edward A.
Groisman, Alex
Deniz, Ashok A.
author_facet Gambin, Yann
Vandelinder, Virginia
Ferreon, Allan Chris M.
Lemke, Edward A.
Groisman, Alex
Deniz, Ashok A.
author_sort Gambin, Yann
collection PubMed
description We combined rapid microfluidic mixing with single-molecule Förster 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 within the encounter complex. The method also enabled study of rapid dissociation and unfolding of weakly bound complexes triggered by massive dilution.
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spelling pubmed-30717992011-09-01 Visualizing a one-way protein encounter complex by ultrafast single-molecule mixing Gambin, Yann Vandelinder, Virginia Ferreon, Allan Chris M. Lemke, Edward A. Groisman, Alex Deniz, Ashok A. Nat Methods Article We combined rapid microfluidic mixing with single-molecule Förster 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 within the encounter complex. The method also enabled study of rapid dissociation and unfolding of weakly bound complexes triggered by massive dilution. 2011-02-06 2011-03 /pmc/articles/PMC3071799/ /pubmed/21297620 http://dx.doi.org/10.1038/nmeth.1568 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Gambin, Yann
Vandelinder, Virginia
Ferreon, Allan Chris M.
Lemke, Edward A.
Groisman, Alex
Deniz, Ashok A.
Visualizing a one-way protein encounter complex by ultrafast single-molecule mixing
title Visualizing a one-way protein encounter complex by ultrafast single-molecule mixing
title_full Visualizing a one-way protein encounter complex by ultrafast single-molecule mixing
title_fullStr Visualizing a one-way protein encounter complex by ultrafast single-molecule mixing
title_full_unstemmed Visualizing a one-way protein encounter complex by ultrafast single-molecule mixing
title_short Visualizing a one-way protein encounter complex by ultrafast single-molecule mixing
title_sort visualizing a one-way protein encounter complex by ultrafast single-molecule mixing
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3071799/
https://www.ncbi.nlm.nih.gov/pubmed/21297620
http://dx.doi.org/10.1038/nmeth.1568
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