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Related Concept Videos

Multi-pass Transmembrane Proteins and β-barrels01:09

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In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
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Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
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Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution
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Hetero-Oligomeric Protein Pores for Single-Molecule Sensing.

Remya Satheesan1, Asuma Janeena1, Kozhinjampara R Mahendran2

  • 1Membrane Biology Laboratory, Rajiv Gandhi Centre for Biotechnology, Transdisciplinary Research Program, Thiruvananthapuram, 695014, India.

The Journal of Membrane Biology
|December 19, 2024
PubMed
Summary
This summary is machine-generated.

Nocardia farcinica porin AB (NfpAB) is a novel hetero-oligomeric nanopore for advanced biomolecular sensing. Its unique structure enables sensitive detection and sequencing of charged molecules, expanding nanopore technology applications.

Keywords:
Nocardia farcinicaCyclodextrinsHetero-oligomericNanoporesPorinsSingle-molecule sensing

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Area of Science:

  • Biotechnology
  • Nanopore Sensing
  • Molecular Biology

Background:

  • Protein nanopores are key single-molecule sensors for DNA and protein sequencing.
  • Current nanopore limitations restrict analyte detection range, hindering broader biotechnological applications.

Purpose of the Study:

  • To review the potential of Nocardia farcinica porin AB (NfpAB), a natural hetero-oligomeric porin, as an advanced nanopore sensor.
  • To highlight NfpAB's unique structural and functional properties for biomolecular detection and sequencing.

Main Methods:

  • Characterization of the NfpAB pore structure formed by NfpA and NfpB subunits.
  • Single-channel electrical recordings to assess channel stability and conductance.
  • Analysis of molecular interaction and translocation kinetics within the pore.

Main Results:

  • NfpAB forms stable, high-conductance channels with unique geometry and charge distribution.
  • The pore effectively senses charged molecules like cationic polypeptides and cyclic sugars.
  • Intrinsic cysteines in NfpAB facilitate thiol-based reactions and molecular adapter attachment.

Conclusions:

  • NfpAB offers enhanced control over molecular interactions and voltage-dependent translocation kinetics.
  • Hetero-oligomeric nanopores like NfpAB show significant promise for biomolecular detection and sequencing.
  • NfpAB represents a versatile platform for advancing nanopore technology.