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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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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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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.
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: Dec 13, 2025

Determining Membrane Protein Topology Using Fluorescence Protease Protection FPP
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Classification of membrane protein using Tetra Peptide Pattern.

A Sherly Alphonse1, N Ani Brown Mary2, M S Starvin3

  • 1Ponjesly College of Engineering, Nagercoil, India.

Analytical Biochemistry
|August 3, 2020
PubMed
Summary
This summary is machine-generated.

Predicting membrane protein function is crucial for understanding biological activity. A new computational method using Tetra Peptide Patterns (TPP) and Deep Belief Networks (DBN) accurately classifies membrane protein types.

Keywords:
Amino acidClassificationFeatureMembrane proteinRBM

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Determining Membrane Protein Topology Using Fluorescence Protease Protection FPP
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Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo
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Area of Science:

  • * Membrane protein research
  • * Computational biology
  • * Bioinformatics

Background:

  • * Membrane proteins are vital for cellular functions and biological activities.
  • * Accurate prediction of membrane protein function is essential for biological research.
  • * Current computational methods require enhancement for timely and precise functional type prediction.

Purpose of the Study:

  • * To develop a novel computational approach for accurate membrane protein functional type prediction.
  • * To introduce a feature extraction technique based on Tetra Peptide Patterns (TPP).
  • * To utilize Deep Belief Networks (DBN) for efficient classification.

Main Methods:

  • * Feature extraction using a novel Tetra Peptide Pattern (TPP) technique.
  • * Dimensionality reduction via General Kernel-based Supervised Principal Component Analysis (GKSPCA).
  • * Classification using Stacked Restricted Boltzmann Machines (RBM) within a Deep Belief Network (DBN).

Main Results:

  • * The proposed method demonstrated strong performance on two independent datasets.
  • * Evaluation metrics included Accuracy, Specificity, Sensitivity, and Mathew's correlation coefficient.
  • * The approach achieved superior results compared to existing state-of-the-art techniques.

Conclusions:

  • * The developed computational method effectively predicts membrane protein functional types.
  • * TPP-based feature extraction combined with DBN offers a powerful approach for membrane protein analysis.
  • * This method accelerates the understanding of cellular mechanisms and biological activities.