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Benjamin Cressiot

Researcher at University of Paris

Publications -  23
Citations -  1017

Benjamin Cressiot is an academic researcher from University of Paris. The author has contributed to research in topics: Nanopore & Medicine. The author has an hindex of 12, co-authored 17 publications receiving 775 citations. Previous affiliations of Benjamin Cressiot include Université Paris-Saclay & Centre national de la recherche scientifique.

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Journal ArticleDOI

Nanopore-Based Measurements of Protein Size, Fluctuations, and Conformational Changes

TL;DR: The measurements reveal a correlation between the mean current blockade amplitude and the radius of gyration for each protein, and the magnitude of the structural fluctuations, as probed by experiments and simulations, correlates with the ratio of α-helix to β-sheet content.
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Dynamics of completely unfolded and native proteins through solid-state nanopores as a function of electric driving force.

TL;DR: The possible phenomena hindering the transport of proteins through the pores, which could explain these anomalous dynamics, are discussed, in particular, electro-osmotic counterflow and protein adsorption on the nanopore wall.
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Protein Transport through a Narrow Solid-State Nanopore at High Voltage: Experiments and Theory

TL;DR: This theory reproduces clearly the experimental crossover between the entropic barrier regime with medium voltage and the electrophoretic regime with higher voltage and suggests that electro-osmotic flow and protein adsorption on the narrowest nanopore wall are minimized.
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Wild Type, Mutant Protein Unfolding and Phase Transition Detected by Single-Nanopore Recording

TL;DR: It is observed that single-nanopore recording can be used as a new single molecule method to explore the unfolding transition and to examine the conformational space of native or variant proteins.
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Differential Enzyme Flexibility Probed Using Solid-State Nanopores

TL;DR: The results unequivocally demonstrate that nanopore-based measurements reliably probe conformational diversity in native protein ensembles.