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Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

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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.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
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Structure of Porins01:21

Structure of Porins

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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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Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

3.0K
Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
3.0K
Protein-protein Interfaces02:04

Protein-protein Interfaces

12.5K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
12.5K
Conserved Binding Sites01:49

Conserved Binding Sites

4.2K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
4.2K
Aquaporins01:25

Aquaporins

4.8K
Aquaporins or AQPs are a family of integral membrane proteins whose primary function is to transport water, while some called aquaglyceroporins also transport glycerol. In addition, aquaporins have also been suspected to be involved in transporting volatile substances, such as carbon dioxide and ammonia, across membranes. Such AQPs that act as gas channels are often highly expressed in cells involved in the gaseous exchange, such as red blood cells, epithelial cells, and pulmonary capillaries.
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Related Experiment Video

Updated: Jun 23, 2025

Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution
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Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution

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Functionally Active Synthetic α-Helical Pores.

Smrithi Krishnan R1, Neilah Firzan Ca1,2, Kozhinjampara R Mahendran1

  • 1Transdisciplinary Research Program, Rajiv Gandhi Centre for Biotechnology, Thiruvananthapuram, India-695014.

Accounts of Chemical Research
|June 14, 2024
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Summary

Researchers created novel synthetic transmembrane α-helical pores using D-amino acids for advanced nanopore sensors. These stable, functional pores offer versatile applications in nanobiotechnology and chemical biology.

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Area of Science:

  • Nanobiotechnology and synthetic chemical biology research.
  • Focus on transmembrane pore engineering for advanced applications.
  • Exploration of synthetic α-helical pores as a novel frontier.

Background:

  • Transmembrane pores are crucial in nanobiotechnology, nanopore chemistry, and synthetic chemical biology.
  • Previous work focused on natural β-barrel pores for sequencing and biomacromolecule sensing.
  • Development of synthetic nanopores is driven by the need for efficient single-molecule detection systems.

Purpose of the Study:

  • To design and construct synthetic transmembrane α-helical pores.
  • To utilize naturally occurring transmembrane motifs for pore fabrication.
  • To develop novel nanopore sensors for single-molecule detection.

Main Methods:

  • Engineering synthetic α-helical transmembrane pores based on the natural porin PorACj.
  • Utilizing computational tools for designing pore structure and functionality.
  • Synthesizing pores using easy chemical methods and incorporating functional groups.
  • Constructing stable pores from D-amino acid peptides for enhanced stability and functionality.

Main Results:

  • Successfully created the first functional, large, and stable synthetic transmembrane pore from short synthetic α-helical peptides.
  • Demonstrated facile chemical synthesis and modification for creating charge-selective pores.
  • Showcased superior stability and functionality of D-amino acid pores compared to L-amino acid pores in the presence of protease.
  • Revealed distinct surface charge conformation and geometry in D- and L-amino acid pores through structural modeling.

Conclusions:

  • Developed novel synthetic α-helical transmembrane pores with unique architecture and functionality.
  • These pores are versatile systems with potential applications in nanopore technology and chemical biology.
  • Potential for use in nanodevices, therapeutic tools, antimicrobial agents, and targeted cancer therapies.