Unfolding and Translocation of Proteins Through an Alpha-Hemolysin Nanopore by ClpXP.

Jeff Nivala, Logan Mulroney, Qing Luan, Robin Abu-Shumays, Mark Akeson

Methods in molecular biology (Clifton, N.J.) 2021

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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.

Citation

Jeff Nivala, Logan Mulroney, Qing Luan, Robin Abu-Shumays, Mark Akeson. Unfolding and Translocation of Proteins Through an Alpha-Hemolysin Nanopore by ClpXP. Methods in molecular biology (Clifton, N.J.). 2021;2186:145-155