ArticleProceedings of the National Academy of Sciences of the United States of America2022
Threading single proteins through pores to compare their energy landscapes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Denoise Stepwise Signals by Diffusion Model-Based Approach.Small methods · 2026Article
- Light-Driven, Phase-Locked Protein Pumping Through a Single Plasmonic Optofluidic Nanopore.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Research progress and application of solid-state nanopore fabrication based on wet etching.Fundamental research · 2026Review
- Digital Immunoassays for Sensitive Quantification of Blood Biomarkers Using Solid-State Nanopores.ACS nano · 2026Article
- Threading of Single Protein Molecules Through a Solid-State Nanopore.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Cell recruitment and the origins of Anterior-Posterior asymmetries in the Drosophila wing.PloS one · 2025Article
- Real-Time Measurement of a Weak Interaction of a Transcription Factor Motif with a Protein Hub at Single-Molecule Precision.ACS nano · 2024Article
- The potential of nanopore technologies toward empowering biophysical research: Brief history, basic principle and applications.Biophysics and physicobiology · 2024Article
- A Marcus-Type Inverted Region in the Translocation Kinetics of a Knotted Protein.The journal of physical chemistry letters · 2023Article
- Article
- A generalizable nanopore sensor for highly specific protein detection at single-molecule precision.Nature communications · 2023Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Translocation of proteins is correlated with structural fluctuations that access conformational states higher in free energy than the folded state. We use electric fields at the solid-state nanopore to control the relative free energy and occupancy of different protein conformational states at the single-molecule level. The change in occupancy of different protein conformations as a function of electric field gives rise to shifts in the measured distributions of ionic current blockades and residence times. We probe the statistics of the ionic current blockades and residence times for three mutants of the [Formula: see text]-repressor family in order to determine the number of accessible conformational states of each mutant and evaluate the ruggedness of their free energy landscapes. Translocation becomes faster at higher electric fields when additional flexible conformations are available for threading through the pore. At the same time, folding rates are not correlated with ease of translocation; a slow-folding mutant with a low-lying intermediate state translocates faster than a faster-folding two-state mutant. Such behavior allows us to distinguish among protein mutants by selecting for the degree of current blockade and residence time at the pore. Based on these findings, we present a simple free energy model that explains the complementary relationship between folding equilibrium constants and translocation rates.
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