Real-time shape approximation and fingerprinting of single proteins using a nanopore
Source abstract
Abstract
Established methods for characterizing proteins typically require physical or chemical modification steps or cannot be used to examine individual molecules in solution. Ionic current measurements through electrolyte-filled nanopores can characterize single native proteins in an aqueous environment, but currently offer only limited capabilities. Here we show that the zeptolitre sensing volume of bilayer-coated solid-state nanopores can be used to determine the approximate shape, volume, charge, rotational diffusion coefficient and dipole moment of individual proteins. To do this, we developed a theory for the quantitative understanding of modulations in ionic current that arise from the rotational dynamics of single proteins as they move through the electric field inside the nanopore. The approach allows us to measure the five parameters simultaneously, and we show that they can be used to identify, characterize and quantify proteins and protein complexes with potential implications for structural biology, proteomics, biomarker detection and routine protein analysis.
Source: europepmc · Quality: candidate unverified · Source record ↗
Research context
OpenAlex topics: Nanopore and Nanochannel Transport Studies · Electrostatics and Colloid Interactions · Ion-surface interactions and analysis
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
References (47)
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