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Related Concept Videos

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...
Structure of Porins01:21

Structure of Porins

Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel precursors...
Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
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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...
Signal Sequences and Sorting Receptors01:41

Signal Sequences and Sorting Receptors

Signal sequences are short amino acid sequences that guide newly synthesized proteins to their proper location within the cell. Classical signal sequences are fifteen to sixty amino acids long and present at the N-terminus of a polypeptide chain. Each signal sequence has a conserved segment of basic residues towards their N terminus, a hydrophobic core, and a C-terminus rich in polar residues. The C-terminus also contains a signal cleavage site and features a -3 -1 sequence motif. The -3-1...
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...

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Related Experiment Video

Updated: Jul 8, 2026

From Constructs to Crystals &#8211; Towards Structure Determination of &#946;-barrel Outer Membrane Proteins
09:55

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins

Published on: July 4, 2016

Current developments on beta-barrel membrane proteins: sequence and structure analysis, discrimination and

M Michael Gromiha1, Makiko Suwa

  • 1Computational Biology Research Center, National Institute of Advanced Industrial Science and Technology, AIST Tokyo Waterfront Bio-IT Research Building, 2-42 Aomi, Koto-ku, Tokyo 135-0064, Japan. michael-gromiha@aist.go.jp

Current Protein & Peptide Science
|January 29, 2008
PubMed
Summary
This summary is machine-generated.

This review details beta-barrel membrane proteins, crucial for transport functions. It explores their structural features and computational methods for identifying these proteins in genomic sequences.

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From Constructs to Crystals &#8211; Towards Structure Determination of &#946;-barrel Outer Membrane Proteins
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Published on: July 4, 2016

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Area of Science:

  • Structural biology
  • Genomics
  • Bioinformatics

Background:

  • Beta-barrel membrane proteins (BOMPs) are vital for cellular transport, but their structural complexity poses challenges for identification.
  • Understanding BOMP structure is key for functional genomics and drug development.

Purpose of the Study:

  • To provide a comprehensive overview of beta-barrel membrane proteins.
  • To describe characteristic features and novel parameters for BOMP folding and stability.
  • To explain computational methods for detecting BOMPs in genomic sequences.

Main Methods:

  • Survey of experimentally determined amino acid sequences and structures.
  • Analysis of characteristic amino acid residue features.
  • Development and application of statistical and machine learning techniques (e.g., neural networks, hidden Markov models).
  • Hydrophobicity profiling and rule-based approaches for predicting membrane-spanning segments.

Main Results:

  • Identified characteristic features of amino acid residues in BOMPs.
  • Developed novel parameters for assessing BOMP folding and stability.
  • Evaluated various computational methods for BOMP discrimination and prediction.
  • Demonstrated the utility of these methods for genome-wide BOMP detection.

Conclusions:

  • Computational approaches, including machine learning, are effective for identifying beta-barrel membrane proteins.
  • This review offers a framework from dataset construction to genome-wide applications for BOMP research.
  • Further research can leverage these methods for a deeper understanding of BOMP functions and structures.