title: Unfolding of proteins and long transient conformations detected by single nanopore recording.
abstract: 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.
authors.affiliation: Laboratoire de Recherche sur les Polymères, équipe Matériaux Polymères aux Interfaces, CNRS-UMR 7581, Université d'Evry, 91025 Evry, France.
authors.forename: G
authors.initials: G
authors.lastname: Oukhaled
authors.forename: J
authors.initials: J
authors.lastname: Mathé
authors.forename: A-L
authors.initials: AL
authors.lastname: Biance
authors.forename: L
authors.initials: L
authors.lastname: Bacri
authors.forename: J-M
authors.initials: JM
authors.lastname: Betton
authors.forename: D
authors.initials: D
authors.lastname: Lairez
authors.forename: J
authors.initials: J
authors.lastname: Pelta
authors.forename: L
authors.initials: L
authors.lastname: Auvray
mesh_terms: D040761:Biomimetic Materials / Q000737:chemistry; D002352:Carrier Proteins / Q000737:chemistry*; D004586:Electrophoresis / Q000379:methods; D029968:Escherichia coli Proteins / Q000737:chemistry; D019791:Guanidine / Q000737:chemistry; D006460:Hemolysin Proteins / Q000737:chemistry*; D058619:Maltose-Binding Proteins; D049329:Nanostructures / Q000737:chemistry*; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D013211:Staphylococcus aureus
chemical_list: D002352:Carrier Proteins; D029968:Escherichia coli Proteins; D006460:Hemolysin Proteins; D058619:Maltose-Binding Proteins; D019791:Guanidine