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Related Concept Videos

Single-pass Transmembrane Proteins01:25

Single-pass Transmembrane Proteins

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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...
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Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

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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...
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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...
6.4K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

11.9K
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
11.9K
Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

4.8K
Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
4.8K
Insertion of Multi-pass Transmembrane Proteins in the RER01:29

Insertion of Multi-pass Transmembrane Proteins in the RER

17.4K
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...
17.4K

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Related Experiment Video

Updated: Jan 11, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

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Small Molecules Targeting the Transmembrane Domain.

Yibo Wang1, Xiaohui Wang1,2

  • 1Laboratory of Chemical Biology, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, Jilin 130022, China.

Journal of Medicinal Chemistry
|November 11, 2025
PubMed
Summary
This summary is machine-generated.

Targeting transmembrane domains (TMDs) of membrane proteins offers new therapeutic avenues. Understanding TMD structure and lipid interactions is key for developing innovative small molecule drugs.

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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
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Area of Science:

  • Biochemistry
  • Structural Biology
  • Pharmacology

Background:

  • Transmembrane domains (TMDs) of membrane proteins are challenging drug targets due to their hydrophobic nature and complex structures.
  • Recent advancements in structural biology and computational methods offer new insights into TMDs.
  • Interactions at the protein-lipid interface present novel opportunities for therapeutic intervention.

Purpose of the Study:

  • To explore the structural characteristics and targeting challenges of TMDs.
  • To investigate mechanisms of small molecule interaction with TMDs within the membrane.
  • To highlight the potential of TMD-targeted therapies and the role of the lipid environment.

Main Methods:

  • Review of structural biology data.
  • Analysis of computational modeling insights.
  • Exploration of small molecule interaction mechanisms (ligand diffusion, partitioning, conformational changes).

Main Results:

  • TMDs present unique structural challenges for drug discovery.
  • Small molecules can modulate TMD function through membrane-based interactions.
  • The lipid environment critically influences membrane protein function.

Conclusions:

  • TMD-targeted drug design holds significant potential for pharmaceutical innovation.
  • Understanding TMD structure and function within the lipid bilayer is crucial for developing effective therapies.
  • Emerging trends indicate a transformative impact of TMD-focused drug discovery on future medicine.