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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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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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Membrane Proteins01:30

Membrane Proteins

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Plasma membranes have integral transmembrane proteins involved in facilitated transport. These proteins are collectively referred to as transport proteins, and they function as either channels for the material or as carriers themselves. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids and a hydrophilic channel through their core that provides a hydrated opening for solutes to pass through the membrane layers. Passage through the channel allows...
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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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Detergent Purification of Membrane Proteins01:18

Detergent Purification of Membrane Proteins

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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...
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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: Nov 24, 2025

Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis
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Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis

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Integrative approach for detecting membrane proteins.

Munira Alballa1,2, Gregory Butler3,4

  • 1Department of Computer Science and Software Engineering, Concordia University, Montreal, QC, Canada. m_alball@encs.concordia.ca.

BMC Bioinformatics
|December 22, 2020
PubMed
Summary
This summary is machine-generated.

This study reveals limitations of current membrane protein detection methods. An integrative approach combining topology prediction and Pse-PSSM optimized OET-KNN predictors significantly improves accuracy for identifying all membrane protein types.

Keywords:
Amino acid compositionIntegral membrane proteinsIntegrative approachMachine learningMembranePrediction modelSurface-bound membrane proteinsTransmembrane

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Area of Science:

  • Bioinformatics
  • Computational Biology
  • Proteomics

Background:

  • Membrane proteins regulate crucial cellular functions.
  • Transmembrane topology prediction tools are commonly used but have limitations.
  • Existing tools often fail to detect surface-bound membrane proteins.

Purpose of the Study:

  • To identify optimal techniques for distinguishing all types of membrane proteins.
  • To address the shortcomings of current prediction tools.
  • To develop a more accurate method for membrane protein identification.

Main Methods:

  • Evaluation of various feature extraction techniques.
  • Comparison of different machine learning algorithms.
  • Development and testing of an integrative approach combining topology prediction and Pse-PSSM optimized OET-KNN predictors.

Main Results:

  • Transmembrane topology prediction tools alone are insufficient for detecting all membrane proteins.
  • An integrative approach combining topology prediction and Pse-PSSM optimized OET-KNN demonstrated superior performance.
  • Cross-validation and independent testing confirmed the effectiveness of the proposed method.

Conclusions:

  • The integrative approach significantly outperforms existing state-of-the-art methods.
  • The developed method achieved 92.51% accuracy in independent testing.
  • This advancement offers improved accuracy and MCC for membrane protein identification.