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Related Concept Videos

Introduction to Membrane Proteins01:16

Introduction to Membrane Proteins

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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...
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Single-pass Transmembrane Proteins01:25

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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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Protein Transport into the Inner Mitochondrial Membrane01:34

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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.
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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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Insertion of Multi-pass Transmembrane Proteins in the RER01:29

Insertion of Multi-pass Transmembrane Proteins in the RER

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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.
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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...
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Related Experiment Video

Updated: Apr 11, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
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TMCompare: transmembrane region sequence and structure.

R C Togawa1, J F Antoniw, J G Mullins

  • 1Bioinformatics Laboratory, Embrapa-Genetic Resources and Biotechnology, Parque Estação Biológico Final Av. W/5 Norte CEP: 70770-900, Caixa Postal: 02372 Brasilia-DF, Brazil. tmcompare@membraneproteins.org

Bioinformatics (Oxford, England)
|December 26, 2001
PubMed
Summary
This summary is machine-generated.

TMCompare aligns and visualizes membrane protein data from SWISS-PROT and PDB files. It detects structural differences, coverage gaps, and annotation discrepancies in transmembrane regions.

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Area of Science:

  • Structural biology
  • Bioinformatics

Background:

  • Membrane proteins are crucial biological components.
  • Discrepancies exist between sequence and structural databases.

Purpose of the Study:

  • To introduce TMCompare, a tool for comparing membrane protein data.
  • To facilitate the analysis of sequence and structural information.

Main Methods:

  • Alignment and visualization of SWISS-PROT and PDB data.
  • Detection of structural breaks in transmembrane regions.
  • Comparison of PDB and SWISS-PROT annotations and coverage.

Main Results:

  • Identified differences in coverage and annotations between databases.
  • Analyzed alpha-helical content within transmembrane regions.
  • Visualized structural variations using the CHIME plugin.

Conclusions:

  • TMCompare aids in identifying discrepancies in membrane protein data.
  • The tool enhances the understanding of transmembrane region structures.