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Multi-pass Transmembrane Proteins and β-barrels01:09

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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.
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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...
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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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Genome-wide Membrane Protein Structure Prediction.

Stefano Piccoli1, Eda Suku1, Marianna Garonzi1

  • 1Applied Bioinformatics Group, Dept. of Biotechnology, University of Verona, strada Le grazie 15, 37134, Verona, Italy;

Current Genomics
|January 10, 2014
PubMed
Summary

Computational approaches, combining structural characterization and bioinformatics, are crucial for understanding membrane proteins. These methods help map the human membrane proteome, overcoming challenges in obtaining high-resolution structures for therapeutic insights.

Keywords:
Genome-wide scale analysisHomology modelingHuman membrane proteomeMembrane protein.Multitasking approachProtein structural bioinformatics

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Bioinformatics

Background:

  • Transmembrane proteins are vital for cellular communication and are key targets for pharmaceutical development.
  • Current genome annotation requires detailed structural and functional characterization of membrane proteins.
  • Obtaining high-resolution 3D structures of membrane proteins is a significant experimental challenge.

Purpose of the Study:

  • To review the integration of structural characterization and bioinformatics for genome-wide membrane protein analysis.
  • To assess the utility of computational approaches in describing the human membrane proteome.
  • To highlight the role of comparative modeling in addressing the lack of experimental structures.

Main Methods:

  • Review of recent advancements in structural characterization of membrane proteins.
  • Application of protein bioinformatics techniques for large-scale analysis.
  • Utilizing comparative modeling to predict 3D structures.

Main Results:

  • Combined structural and bioinformatics efforts offer a scalable approach to membrane protein characterization.
  • Comparative modeling shows promise in overcoming the limitations of experimental structure determination.
  • These integrated methods can contribute to a comprehensive understanding of the human membrane proteome.

Conclusions:

  • Computational strategies are essential for advancing the study of membrane proteins at a genome-wide scale.
  • Comparative modeling is a valuable tool for structural and functional annotation of the human membrane proteome.
  • This integrated approach facilitates the identification of potential therapeutic targets.