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Updated: Dec 9, 2025

Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution
Published on: August 16, 2016
Unfolding and Translocation of Proteins Through an Alpha-Hemolysin Nanopore by ClpXP
Jeff Nivala1, Logan Mulroney2, Qing Luan3
1Paul G. Allen School of Computer Science and Engineering, University of Washington, Seattle, WA, USA. jmdn@uw.edu.
Abstract:
Proteins present a significant challenge for nanopore-based sequence analysis. This is partly due to their stable tertiary structures that must be unfolded for linear translocation, and the absence of regular charge density. To address these challenges, here we describe how ClpXP, an ATP-dependent protein unfoldase, can be harnessed to unfold and processively translocate multi-domain protein substrates through an alpha-hemolysin nanopore sensor. This process results in ionic current patterns that are diagnostic of protein sequence and structure at the single-molecule level.
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