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Single-pass Transmembrane Proteins

Single-pass Transmembrane Proteins

Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...

Protein Diffusion in the Membrane

Protein Diffusion in the Membrane

Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...

Multi-pass Transmembrane Proteins and β-barrels

Multi-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...

Insertion of Single-pass Transmembrane Proteins in the RER

Insertion of Single-pass Transmembrane Proteins in the RER

Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...

Directing Proteins to the Rough Endoplasmic Reticulum

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...

Insertion of Multi-pass Transmembrane Proteins in the RER

Insertion of Multi-pass Transmembrane Proteins in the RER

The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...

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Related Experiment Video

Updated: Jul 14, 2026

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

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

Published on: August 16, 2016

A rational route to probing membrane proteins.

Amy E Keating¹

¹MIT Department of Biology, Massachusetts Avenue, Cambridge, MA 02139, USA. keating@mit.edu

|June 2, 2007

Summary

Researchers designed short peptides that specifically bind to transmembrane regions of integrins. This offers a new tool for studying membrane protein biology.

Area of Science:

Biochemistry
Molecular Biology
Cell Biology

Background:

Integrins are crucial cell surface receptors involved in cell adhesion and signaling.
Understanding integrin function requires tools to specifically target their transmembrane domains.
Membrane proteins play vital roles in cellular processes but are challenging to study.

Purpose of the Study:

To design and characterize novel short peptides with specific binding affinity for integrin transmembrane regions.
To develop a new molecular tool for investigating the biological roles of integrins and other membrane proteins.

Main Methods:

Peptide library design and synthesis.
Biochemical assays to assess binding specificity and affinity.
Cell-based assays to evaluate peptide interactions with native integrins.

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Tracking Single Proteins in Lipid Bilayers Using Fluorescence Microscopy

Tracking Single Proteins in Lipid Bilayers Using Fluorescence Microscopy

Published on: December 12, 2025

Determining Membrane Protein Topology Using Fluorescence Protease Protection (FPP)

Determining Membrane Protein Topology Using Fluorescence Protease Protection (FPP)

Published on: April 20, 2015

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Last Updated: Jul 14, 2026

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

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

Published on: August 16, 2016

Tracking Single Proteins in Lipid Bilayers Using Fluorescence Microscopy

Tracking Single Proteins in Lipid Bilayers Using Fluorescence Microscopy

Published on: December 12, 2025

Determining Membrane Protein Topology Using Fluorescence Protease Protection (FPP)

Determining Membrane Protein Topology Using Fluorescence Protease Protection (FPP)

Published on: April 20, 2015

Main Results:

Successfully designed and validated short peptides exhibiting high specificity for integrin transmembrane domains.
Demonstrated the utility of these peptides in probing integrin-mediated cellular processes.
Established a novel method for targeting membrane protein domains.

Conclusions:

The developed peptides represent a significant advancement in the study of integrin biology.
These peptides provide a versatile tool for exploring the function of transmembrane proteins.
This work opens new avenues for therapeutic strategies targeting integrin function.