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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...
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...
Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
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...
Fluid Mosaic Model01:19

Fluid Mosaic Model

Scientists identified the plasma membrane in the 1890s and its principal chemical components (lipids and proteins) by 1915. The model for plasma membrane structure, proposed in 1935 by Hugh Davson and James Danielli, was the first model to be widely accepted in the scientific community. The model was based on the plasma membrane's "railroad track" appearance in early electron micrographs. Davson and Danielli theorized that the plasma membrane's structure resembled a sandwich with the analogy of...
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...

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A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

SOMPNN: an efficient non-parametric model for predicting transmembrane helices.

Dong-Jun Yu1, Hong-Bin Shen, Jing-Yu Yang

  • 1School of Computer Science, Nanjing University of Science and Technology, 200 Xiaolingwei Road, Nanjing, 210094, China.

Amino Acids
|June 23, 2011
PubMed
Summary
This summary is machine-generated.

This study introduces a novel SOMPNN model for predicting transmembrane helices (TMH) in proteins. The model offers high accuracy with minimal parameters and improved efficiency for TMH prediction.

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Area of Science:

  • Bioinformatics
  • Computational Biology
  • Structural Biology

Background:

  • Accurate prediction of transmembrane helices (TMH) in helical membrane proteins is crucial but challenging.
  • Existing parametric TMH predictors often require extensive parameter assumptions and can be computationally inefficient, especially with large datasets.

Purpose of the Study:

  • To develop a novel Self-Organizing Map-Probabilistic Neural Network (SOMPNN) model for enhanced TMH prediction.
  • To address the limitations of parametric models by reducing parameter assumptions and increasing computational efficiency.

Main Methods:

  • Utilized a Self-Organizing Map (SOM) to learn helix distribution patterns from training data.
  • Employed a Probabilistic Neural Network (PNN) for TMH segment prediction based on SOM-derived knowledge.
  • Developed a novel SOMPNN model with minimal parameter requirements and high computational efficiency.

Main Results:

  • The SOMPNN model demonstrated superior performance compared to existing popular TMH predictors on two benchmark datasets.
  • Achieved accurate prediction of transmembrane helices with reduced reliance on parameter assumptions.
  • Showcased high computational efficiency, making it suitable for large-scale biological data analysis.

Conclusions:

  • The proposed SOMPNN model is a promising advancement for transmembrane helix prediction.
  • The model's efficiency and accuracy suggest potential for application to other complex biological problems.
  • Datasets and source code are publicly available for further research and development.