Document Detail


Dynamics of Unfolded Protein Transport through an Aerolysin Pore.
MedLine Citation:
PMID:  21319816     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Protein export is an essential mechanism in living cells and exported proteins are usually translocated through a protein-conducting channel in an unfolded state. Here we analyze, by electrical detection, the entry and transport of unfolded proteins, at the single molecule level, with different stabilities through an aerolysin pore, as a function of the applied voltage and protein concentration. The frequency of ionic current blockades varies exponentially as a function of the applied voltage and linearly as a function of protein concentration. The transport time of unfolded proteins decreases exponentially when the applied voltage increases. We prove that the ionic current blockade duration of a double-sized protein is longer than that assessed for a single protein supporting the transport phenomenon. Our results fit with the theory of confined polyelectrolyte and with some experimental results about DNA or synthetic polyelectrolyte translocation through protein channels as a function of applied voltage. We discuss the potential of the aerolysin nanopore as a tool for protein folding studies as it has already been done for α-hemolysin.
Authors:
Manuela Pastoriza-Gallego; Leila Rabah; Gabriel Gibrat; Bénédicte Thiebot; Françoise Gisou van der Goot; Loïc Auvray; Jean-Michel Betton; Juan Pelta
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-2-14
Journal Detail:
Title:  Journal of the American Chemical Society     Volume:  -     ISSN:  1520-5126     ISO Abbreviation:  -     Publication Date:  2011 Feb 
Date Detail:
Created Date:  2011-2-15     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7503056     Medline TA:  J Am Chem Soc     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
Equipe Matériaux Polymères aux Interfaces, CNRS-UMR 8587, LAMBE, Université d'Évry , Bd F. Mitterrand, 91025 Évry France.
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