Related Experiment Video
Updated: Oct 14, 2025
11:55
Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution
Published on: August 16, 2016
11.8K
Challenges and approaches to studying pore-forming proteins
Joshua T Benton1,2, Charles Bayly-Jones1,2
1Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria, Australia.
Biochemical Society Transactions
|November 8, 2021
Summary
Pore-forming proteins (PFPs) are vital for defense and have diverse applications. Studying PFPs using advanced methods like cryo-electron microscopy (cryoEM) and single-molecule techniques is crucial for developing engineered PFPs.
Area of Science:
- Biochemistry and Molecular Biology
- Immunology
- Biotechnology
Background:
- Pore-forming proteins (PFPs) are a diverse class of molecules with critical roles in natural defense mechanisms, particularly within the human immune system.
- PFPs exhibit varied families, structural folds, and assembly pathways, highlighting their complexity.
Purpose of the Study:
- To review the current challenges, knowledge gaps, and emerging approaches in the study of pore-forming proteins.
- To emphasize the importance of overcoming these challenges for the development of custom-engineered PFPs with novel properties.
Main Methods:
- Cryo-electron microscopy (cryoEM) has significantly advanced PFP research.
- Emerging single-molecule techniques and methods are being employed to address outstanding questions in PFP studies.
Main Results:
- Despite advancements, significant challenges and knowledge gaps persist in understanding PFP structure, function, and assembly.
- The review consolidates current understanding and highlights areas requiring further investigation.
Conclusions:
- Continued research employing advanced techniques is essential for a comprehensive understanding of PFPs.
- Addressing current limitations will facilitate the rational design and engineering of PFPs for diverse applications, including medicine, agriculture, and biosensing.
Related Concept Videos
01:21Structure of Porins
3.4K
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...
3.4K
01:09Multi-pass Transmembrane Proteins and β-barrels
5.9K
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...
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
5.9K
01:17Pore Transport and Ion-Pair Transport
750
Pore transport and ion-pair formation are critical mechanisms for the absorption and distribution of drugs in the body.
Pore transport, also known as convective transport, is a process where small molecules like urea, water, and sugars rapidly cross cell membranes as though there were channels or pores in the membrane. Although direct microscopic evidence is limited but the concept of pores or channels is widely accepted based on physiological evidence. Despite the lack of direct...
Pore transport, also known as convective transport, is a process where small molecules like urea, water, and sugars rapidly cross cell membranes as though there were channels or pores in the membrane. Although direct microscopic evidence is limited but the concept of pores or channels is widely accepted based on physiological evidence. Despite the lack of direct...
750
02:04Protein-protein Interfaces
14.0K
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...
14.0K
01:16Introduction to Membrane Proteins
74.8K
The cell membrane, or plasma membrane, is an ever-changing landscape. It is described as a fluid mosaic where various macromolecules are embedded in the phospholipid bilayer. Among the macromolecules are proteins. The protein content varies across cell types. For example, mitochondrial inner membranes contain ~76% protein content, while myelin contains ~18% protein content. Individual cells contain many types of membrane proteins—red blood cells contain over 50—and different cell...
74.8K
01:12Porin Insertion in the Outer Mitochondrial Membrane
3.6K
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...
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...
3.6K