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1.
Phys Rev Lett ; 100(15): 158302, 2008 Apr 18.
Article in English | MEDLINE | ID: mdl-18518160

ABSTRACT

We study the transport of dextran sulfate through a protein channel as a function of applied voltage. Below 60 mV, the chain's entrance to the pore is hindered by an entropic barrier; above 60 mV, the strong local electric field forces the chain entrance. The effective charge of the polyelectrolyte inside the pore is reduced. We observe two types of blockades which have durations that decrease when the applied voltage increases. The shortest is a straddling time between the polyelectrolyte and the pore; the longest is the translocation time. The translocation time obeys an exponential dependence upon applied voltage.


Subject(s)
Dextran Sulfate/chemistry , Hemolysin Proteins/chemistry , DNA, Single-Stranded/chemistry , Electrochemistry , Entropy , Lipid Bilayers/chemistry , Osmolar Concentration
2.
Phys Rev Lett ; 98(15): 158101, 2007 Apr 13.
Article in English | MEDLINE | ID: mdl-17501386

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.


Subject(s)
Carrier Proteins/chemistry , Hemolysin Proteins/chemistry , Nanostructures/chemistry , Protein Folding , Biomimetic Materials/chemistry , Electrophoresis/methods , Escherichia coli Proteins/chemistry , Guanidine/chemistry , Maltose-Binding Proteins , Protein Conformation , Protein Denaturation , Staphylococcus aureus
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