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Lipids as Anchors

Lipids 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...

Tagging and Fusion Proteins

Tagging and Fusion Proteins

Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...

Tail-anchoring of Proteins in the ER Membrane

Tail-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...

GPI Anchoring of Proteins in the ER Membrane

GPI Anchoring of Proteins in the ER Membrane

GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...

Immunoprecipitation

Immunoprecipitation

Immunoprecipitation, or IP, is a widely used technique that employs protein-antibody interactions to isolate proteins or protein complexes in their native state for studying protein-protein interactions, quaternary structures, or supramolecular complexes. Various modifications of the technique, including chromatin IP, cross-linking IP, and fluorescence IP, are commonly used.
Chromatin Immunoprecipitation
Chromatin immunoprecipitation, also known as ChIP, is used to study protein-DNA or...

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Related Experiment Video

Updated: May 31, 2026

Functional Surface-immobilization of Genes Using Multistep Strand Displacement Lithography

Functional Surface-immobilization of Genes Using Multistep Strand Displacement Lithography

Published on: October 25, 2018

Self-aligned immobilization of proteins utilizing PEG patterns.

Lap Man Lee¹, Ronald L Heimark, James C Baygents

¹Department of Aerospace and Mechanical Engineering, University of Arizona, Tucson, AZ 85719, USA.

|July 6, 2011

Summary

Researchers developed a new method for precisely attaching proteins to silicon dioxide surfaces. This technique uses photolithography and a polyethylene glycol (PEG) layer to control where proteins bind, preventing unwanted attachment.

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Last Updated: May 31, 2026

Functional Surface-immobilization of Genes Using Multistep Strand Displacement Lithography

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Published on: October 25, 2018

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy

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OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

Published on: February 5, 2020

Area of Science:

Biomaterials Science
Surface Chemistry
Microfabrication

Background:

Selective protein immobilization is crucial for biosensors and tissue engineering.
Existing methods often lack precision or require complex steps.
Controlling bio-specific and non-specific interactions on surfaces is a significant challenge.

Purpose of the Study:

To develop a self-aligned, photolithographic method for selective protein immobilization on silicon dioxide.
To create surfaces with distinct regions for targeted binding and bio-fouling resistance.
To characterize the properties of the resulting functionalized surfaces.

Main Methods:

A standard lift-off patterning technique was employed using a polyethylene glycol (PEG) layer.
Photolithography was used to define regions for protein binding.
Derivatization of silicon dioxide surfaces to enable selective immobilization was performed.

Main Results:

A novel self-aligned method for selective protein immobilization was successfully developed.
Patterned regions demonstrated specific binding of target proteins and particles.
Surrounding regions effectively suppressed non-specific attachment of biological species.
Characterization confirmed the physical and biological integrity of the derivatized surfaces.

Conclusions:

The developed method offers precise control over protein immobilization on silicon dioxide surfaces.
This technique enables the creation of bio-interfaces with tailored functionalities.
The approach holds potential for applications in diagnostics, drug delivery, and regenerative medicine.