ArticleEuropean biophysics journal : EBJ2008
Excursion of a single polypeptide into a protein pore: simple physics, but complicated biology.
Article in European biophysics journal : EBJ, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 75 citations in OpenAlex.
- Review
- Current noise of a protein-selective biological nanopore.Proteomics · 2022Article
- Automated Electrical Quantification of Vitamin B1 in a Bodily Fluid using an Engineered Nanopore Sensor.Angewandte Chemie (International ed. in English) · 2021Article
- Protein identification by nanopore peptide profiling.Nature communications · 2021Article
- Nanopore sensing: A physical-chemical approach.Biochimica et biophysica acta. Biomembranes · 2021Review
- Kinetics of the multitasking high-affinity Win binding site of WDR5 in restricted and unrestricted conditions.The Biochemical journal · 2021Article
- Insertion state of modular protein nanopores into a membrane.Biochimica et biophysica acta. Biomembranes · 2021Article
- Label-Free Detection of Post-translational Modifications with a Nanopore.Nano letters · 2019Article
- Single-Molecule Protein Detection in a Biofluid Using a Quantitative Nanopore Sensor.ACS sensors · 2019Article
- Article
- Paving the way to single-molecule protein sequencing.Nature nanotechnology · 2018Review
- Effects of Nanopore Charge Decorations on the Translocation Dynamics of DNA.Biophysical journal · 2017Article
- Aberrantly Large Single-Channel Conductance of Polyhistidine Arm-Containing Protein Nanopores.Biochemistry · 2017Article
- Interference-Free Detection of Genetic Biomarkers Using Synthetic Dipole-Facilitated Nanopore Dielectrophoresis.ACS nano · 2017Article
- The Transmembrane Domain of a Bicomponent ABC Transporter Exhibits Channel-Forming Activity.ACS chemical biology · 2016Article
- Dynamics and Energy Contributions for Transport of Unfolded Pertactin through a Protein Nanopore.ACS nano · 2015Article
- Membrane Protein Structure, Function, and Dynamics: a Perspective from Experiments and Theory.The Journal of membrane biology · 2015Review
- Quasithermodynamic contributions to the fluctuations of a protein nanopore.ACS chemical biology · 2015Article
- Nanopore-based fourth-generation DNA sequencing technology.Genomics, proteomics & bioinformatics · 2015Review
- Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Despite its fundamental and critical importance in molecular biology and practical medical biotechnology, how a polypeptide interacts with a transmembrane protein pore is not yet comprehensively understood. Here, we employed single-channel electrical recordings to reveal the interactions of short polypeptides and small folded proteins with a robust beta-barrel protein pore. The short polypeptides were approximately 25 residues in length, resembling positively charged targeting presequences involved in protein import. The proteins were consisted of positively charged pre-cytochrome b2 fragments (pb2) fused to the small ribonuclease barnase (approximately 110 residues, Ba). Single-molecule experiments exploring the interaction of a folded pb2-Ba protein with a single beta-barrel pore, which contained negatively charged electrostatic traps, revealed the complexity of a network of intermolecular forces, including driving and electrostatic ones. In addition, the interaction was dependent on other factors, such as the hydrophobic content of the interacting polypeptide, the location of the electrostatic trap, the length of the pb2 presequence and temperature. This single-molecule approach together with protein design of either the interacting polypeptide or the pore lumen opens new opportunities for the exploration of the polypeptide-pore interaction at high temporal resolution. Such future studies are also expected to unravel the advantages and limitations of the nanopore technique for the detection and exploration of individual polypeptides.
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