Evidence map›Paper›PMID 41649957›Full record

ArticleNano letters2026

Uncovering Hidden Protein Conformations with High Bandwidth Nanopore Measurements.

Kyril Kavetsky, Sabine Hong, Chih-Yuan Lin, Roger Yang, Marija Drndić

Abstract read
In one paragraph

Article in Nano letters, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Nanopore event detection in a simple and adaptive way.bioRxiv : the preprint server for biology · 2026
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Kyril KavetskyDepartment of Physics and Astronomy, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.ORCID 0000-0001-7213-1219
Sabine HongDepartment of Physics and Astronomy, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.
Chih-Yuan LinDepartment of Physics and Astronomy, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.ORCID 0000-0002-2425-5548
Roger YangDepartment of Physics and Astronomy, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.
Marija DrndićDepartment of Physics and Astronomy, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.ORCID 0000-0002-8104-2231

Funding

ChimeraX -- Next Generation Visualization and Analysis Software for Multiscale ModelingR01GM129325 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2018 to 2025
$5.2M
Enzymeless, controlled electrostatic ratcheting in solid-state nanoporesR01HG012413 · NHGRI · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI DRNDIC, MARIJA, SHEPARD, KENNETH L · 2022 to 2025
$3.1M
Exploring 3Dpol for RNA sequencing in real timeR21HG011120 · NHGRI · THOMAS JEFFERSON UNIVERSITY · PI HOU, YA-MING · 2020 to 2022
$624k
Advanced Parallel Readers for DNA Sequencing Through a 2D NanoporeR21HG012395 · NHGRI · UNIVERSITY OF PENNSYLVANIA · PI DRNDIC, MARIJA · 2022 to 2023
$424k
National Science Foundation DMR-1720530NHGRI NIH HHS R01 HG01241NHGRI NIH HHS R01 HG012413NHGRI NIH HHS R21 HG011120NHGRI NIH HHS R21 HG012395NIGMS NIH HHS R01 GM129325NIH HHS R01-GM129325NSF NNCI-1542153University of Pennsylvania Materials Research Science and Engineering Center
6 · The paper itself

Abstract

Advanced nanopore measurements allow structural probing of molecules with high spatial and temporal resolution. We report high signal-to-noise, 1-10 MHz bandwidth, translocation measurements of the multistate folding of heme protein cytochrome c in KCl solution through optimally designed silicon nitride pores of 2.3 - 3.3 nm diameter and 3.6-3.8 nm effective thickness, and an optimal concentration of a denaturant (Gdm-Cl). The pore diameter is slightly smaller than the protein's size, forcing the protein to squeeze through the pore. The sufficiently large pore thickness allows enough time for protein probing at an applied field of ∼ 250 kV/cm. Through Bayesian Information Criterion score analysis, current blockades reveal six distinct levels, attributed to specific protein states. We calculate the transition probabilities between the states and the conditional probabilities of the protein leaving the pore from each state. We validate the model by simulating events and comparing them with experimental data.

Indexed as

Cytochromes cNanoporesProtein ConformationProtein FoldingSilicon CompoundsCytochromes cSilicon Compoundssilicon nitridehigh bandwidthlow noise amplifierNanoporeprotein foldingsingle moleculeultrafast protein translocation

Identifiers

PMID41649957
PMCPMC13531597

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.