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

被引:245
作者
Oukhaled, G.
Mathe, J.
Biance, A. -L.
Bacri, L.
Betton, J. -M.
Lairez, D.
Pelta, J. [1 ]
Auvray, L.
机构
[1] Univ Evry, CNRS, UMR 7581, Lab Rech Polymeres,Equipe Mat Polymeres Interface, F-91025 Evry, France
[2] Inst Pasteur, URA 2185, CNRS, Unite Biochim Struct, F-75724 Paris 15, France
[3] CEA Saclay, Lab Leon Brillouin, CNRS, F-91191 Gif Sur Yvette, France
[4] Univ Cergy Pontoise, Grp Microenvironm & Comportements Cellulaires, F-95302 Cergy Pontoise, France
关键词
D O I
10.1103/PhysRevLett.98.158101
中图分类号
O4 [物理学];
学科分类号
0702 ;
摘要
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.
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页数:4
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