ArticleArXiv2025
Uncovering hidden protein conformations with high bandwidth nanopore measurements.
Article in ArXiv, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Authors and funding
5 authors.
Funding
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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 multi-state 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 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 approximately 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 to experimental data.
Identifiers
41445816PMC12723782What OpenQuestion holds
Registered trials
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.