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Protein Unfolding Through Nanopores

Abstract : In this mini-review we introduce and discuss a new method, at single molecule level, to study the protein fold-ing and protein stability, with a nanopore coupled to an electric detection. Proteins unfolded or partially folded passing through one channel submitted to an electric field, in the presence of salt solution, induce different detectable blockades of ionic current. Their duration depends on protein conformation. For different studies proteins through nanopores, com-pletely unfolded proteins induce only short current blockades. Their frequency increases as the concentration of denatur-ing agent or temperature increases, following a sigmoidal denaturation curve. The geometry or the net charge of the nanopores does not alter the unfolding transition, sigmoidal unfolding curve and half denaturing concentration or half temperature denaturation. A destabilized protein induces a shift of the unfolding curve towards the lower values of the de-naturant agent compared to the wild type protein.Partially folded proteins exhibit very long blockades in nanopores. The blockade duration decreases when the concentration of denaturing agent increases. The variation of these blockades could be associated to a possible glassy behaviour.
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Contributor : Laurent Bacri <>
Submitted on : Monday, February 4, 2019 - 4:11:25 PM
Last modification on : Tuesday, May 19, 2020 - 12:09:28 PM


  • HAL Id : hal-02006485, version 1


Abdelghani Oukhaled, Manuela Pastoriza-Gallego, Laurent Bacri, Jérôme Mathé, Loïc Auvray, et al.. Protein Unfolding Through Nanopores. Protein & Peptide Letters, 2014, 21 (3), pp.266-274. ⟨hal-02006485⟩



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