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Related Concept Videos

Single-pass Transmembrane Proteins01:25

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

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...
Multi-pass Transmembrane Proteins and β-barrels01:09

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 Multi-pass Transmembrane Proteins in the RER01:29

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...
Introduction to Membrane Proteins01:16

Introduction to Membrane Proteins

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 types have...
Membrane Proteins01:30

Membrane Proteins

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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Updated: May 15, 2026

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

A simple method for predicting transmembrane proteins based on wavelet transform.

Bin Yu1, Yan Zhang

  • 1College of Mathematics and Physics, Qingdao University of Science and Technology, Qingdao, Shandong, China. yubin@qust.edu.cn

International Journal of Biological Sciences
|January 5, 2013
PubMed
Summary
This summary is machine-generated.

This study introduces a new discrete wavelet transform (DWT) method for accurately predicting transmembrane helical segments (TMHs) in membrane proteins, improving upon existing prediction techniques.

Keywords:
Discrete wavelet transformHydrophobicity.Membrane proteinTransmembrane helical segments

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Determining Membrane Protein Topology Using Fluorescence Protease Protection (FPP)
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Area of Science:

  • Bioinformatics
  • Computational Biology
  • Structural Biology

Background:

  • The rapid increase in protein sequence data necessitates advanced theoretical methods for predicting transmembrane helical segments (TMHs).
  • Existing TMH prediction methods often exhibit limitations in accuracy and adaptability.
  • Accurate TMH prediction is crucial for understanding membrane protein structure and function.

Purpose of the Study:

  • To develop and validate a novel computational method for predicting the number and location of TMHs in membrane proteins.
  • To address the deficiencies in accuracy and adaptability of current TMH prediction tools.
  • To provide a reliable theoretical approach for analyzing membrane protein topology.

Main Methods:

  • A prediction method based on discrete wavelet transform (DWT) was developed.
  • The method was applied to predict TMHs in membrane protein sequences from the Mptopo database (80 proteins, 325 TMHs).
  • Predictions were validated using a test set of 80 membrane protein sequences.

Main Results:

  • The DWT-based method achieved a prediction accuracy of 96.3% on the test set, correctly predicting 308 TMHs.
  • Satisfactory prediction results were obtained when applied to different functional and type groups of membrane proteins.
  • Comparative analysis showed higher prediction accuracy compared to seven popular existing prediction methods.

Conclusions:

  • The proposed discrete wavelet transform (DWT) method demonstrates superior accuracy and adaptability for predicting TMHs in membrane proteins.
  • This method offers a significant advancement in the theoretical prediction of membrane protein topology.
  • The findings suggest a promising new tool for bioinformatics and structural biology research.