Related Experiment Video
Updated: May 10, 2026
10:49
Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
Published on: March 5, 2017
Tripod Amphiphiles for Membrane Protein Manipulation.
Pil Seok Chae1, Philip D Laible, Samuel H Gellman
1Department of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI 53706 (USA). ; Tel: (+1) 608-262-3303.
Molecular Biosystems
|July 2, 2013
Summary
Researchers are developing novel "tripod amphiphiles" as alternatives to traditional detergents for studying integral membrane proteins (IMPs). These new compounds aim to improve the solubilization and crystallization of these challenging but vital biological molecules.
Area of Science:
- Biochemistry
- Structural Biology
- Organic Chemistry
Background:
- Integral membrane proteins (IMPs) are essential for cellular functions but difficult to isolate and study.
- Limited high-resolution structural data exists for IMPs due to challenges in obtaining soluble, active, and crystallizable protein preparations.
- Conventional detergents are used for IMP solubilization, but many proteins remain recalcitrant.
Purpose of the Study:
- To report progress on developing a new class of amphiphiles, termed "tripod amphiphiles."
- To provide alternatives to conventional detergents for manipulating integral membrane proteins.
- To identify novel amphiphiles that facilitate IMP crystallization.
Main Methods:
- Development of novel organic molecules: "tripod amphiphiles."
- Evaluation of tripod amphiphiles as alternatives to conventional detergents for IMP solubilization.
- Exploration of amphiphile properties for facilitating IMP crystallization.
Main Results:
- Tripod amphiphiles are a new class of organic molecules designed for membrane protein manipulation.
- These amphiphiles are intended as alternatives to conventional detergents.
- The research aims to identify amphiphiles that improve IMP crystallization.
Conclusions:
- New amphiphiles, such as tripod amphiphiles, are needed for integral membrane protein research.
- Developing novel amphiphiles could overcome current limitations in studying IMPs.
- This work highlights a critical need in biochemistry and may inspire new chemical approaches.
Related Concept Videos
01:18Detergent Purification of Membrane Proteins
Detergents are used to purify the integral proteins of the membrane. The hydrophobic portion of the detergent can replace membrane phospholipids while solubilizing the membrane proteins. When detergent monomers reach a specific concentration in a solution called critical micelle concentration (CMC), they form micelles. Above CMC, the concentration of the detergent monomers remains in equilibrium with the micelle. The number of detergent monomers present in the CMC varies for each detergent, and...
01:39Mechanism of Filopodia Formation
Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
01:15Mechanisms of Membrane-bending
The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
Membrane bending can happen due to intrinsic changes in lipid composition or extrinsic association with different proteins. The proteins involved...
Membrane bending can happen due to intrinsic changes in lipid composition or extrinsic association with different proteins. The proteins involved...
01:32Lipids as Anchors
In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains the...
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains the...
01:09Multi-pass Transmembrane Proteins and β-barrels
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 G-protein-linked receptors (GPCRs) and...
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
01:45Tail-anchoring of Proteins in the ER Membrane
Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...