ArticleMethods in molecular biology (Clifton, N.J.)2012
Protein sensing with engineered protein nanopores.
Article in Methods in molecular biology (Clifton, N.J.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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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.
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- A Nanopore Approach for Analysis of Caspase-7 Activity in Cell Lysates.Biophysical journal · 2019Article
- Information Dynamics of a Nonlinear Stochastic Nanopore System.Entropy (Basel, Switzerland) · 2018Article
- Porphyrin-Assisted Docking of a Thermophage Portal Protein into Lipid Bilayers: Nanopore Engineering and Characterization.ACS nano · 2017Article
- Label-Free and Real-Time Detection of Protein Ubiquitination with a Biological Nanopore.ACS nano · 2017Article
- Genomic Pathogen Typing Using Solid-State Nanopores.PloS one · 2015Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The use of nanopores is a powerful new frontier in single-molecule sciences. Nanopores have been used effectively in exploring various biophysical features of small polypeptides and proteins, such as their folding state and structure, ligand interactions, and enzymatic activity. In particular, the α-hemolysin (αHL) protein pore has been used extensively for the detection, characterization, and analysis of polypeptides because this protein nanopore is highly robust, versatile, and tractable under various experimental conditions. Inspired by the mechanisms of protein translocation across the outer membrane translocases of mitochondria, we have shown the ability to use nanopore-probe techniques in controlling a single protein using engineered αHL pores. Here, we provide a detailed protocol for the preparation of αHL protein nanopores. Moreover, we demonstrate that placing attractive electrostatic traps is instrumental in tackling single-molecule stochastic sensing of folded proteins.
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Registered trials
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