Unfolding of proteins and long transient conformations detected by single nanopore recording

We study the electrophoretic blockades due to entries of partially unfolded proteins into a nanopore as a function of the concentration of the denaturing agent. Short and long pore blockades are observed by electrical detection. Short blockades are due to the passage of completely unfolded proteins,...

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Bibliographic Details
Published in:Physical review letters 2007-04, Vol.98 (15), p.158101-158101, Article 158101
Main Authors: Oukhaled, G, Mathé, J, Biance, A-L, Bacri, L, Betton, J-M, Lairez, D, Pelta, J, Auvray, L
Format: Article
Language:English
Subjects:
Biomimetic Materials - chemistry
Carrier Proteins - chemistry
Condensed Matter
Electrophoresis - methods
Escherichia coli Proteins - chemistry
Guanidine - chemistry
Hemolysin Proteins - chemistry
Maltose-Binding Proteins
Nanostructures - chemistry
Physics
Protein Conformation
Protein Denaturation
Protein Folding
Soft Condensed Matter
Staphylococcus aureus
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Summary:We study the electrophoretic blockades due to entries of partially unfolded proteins into a nanopore as a function of the concentration of the denaturing agent. Short and long pore blockades are observed by electrical detection. Short blockades are due to the passage of completely unfolded proteins, their frequency increases as the concentration of the denaturing agent increases, following a sigmoidal denaturation curve. Long blockades reveal partially folded conformations. Their duration increases as the proteins are more folded. The observation of a Vogel-Fulcher law suggests a glassy behavior.
ISSN:0031-9007
1079-7114
DOI:10.1103/physrevlett.98.158101