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Related Concept Videos

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
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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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Structure of Porins01:21

Structure of Porins

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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...
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Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

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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...
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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 Fluidity01:23

Membrane Fluidity

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Cell membranes are composed of phospholipids, proteins, and carbohydrates loosely attached to one another through chemical interactions. Molecules are generally able to move about in the plane of the membrane, giving the membrane its flexible nature called fluidity. Two other features of the membrane contribute to membrane fluidity: the chemical structure of the phospholipids and the presence of cholesterol in the membrane.
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Updated: Aug 5, 2025

From Constructs to Crystals &#8211; Towards Structure Determination of &#946;-barrel Outer Membrane Proteins
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From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins

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3D-BMPP: 3D Beta-Barrel Membrane Protein Predictor.

Wei Tian1, Meishan Lin1, Ke Tang1

  • 1Center for Bioinformatics and Quantitative Biology and Richard and Loan Hill Department of Biomedical Engineering, University of Illinois at Chicago, Chicago, IL, USA.

Methods in Molecular Biology (Clifton, N.J.)
|March 24, 2023
PubMed
Summary
This summary is machine-generated.

We developed 3D-BMPP, a novel method for predicting the 3D structures of beta-barrel membrane proteins (βMPs). This tool accurately models transmembrane domains and extended beta barrels, advancing structural biology research.

Keywords:
Computer simulationLoop predictionSequence covariationSequential Monte Carlo samplingStrand registerStructure predictionβ-barrel membrane proteins

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Area of Science:

  • Structural biology
  • Biochemistry
  • Genomics

Background:

  • Beta-barrel membrane proteins (βMPs) are crucial in cellular membranes but experimentally challenging to study.
  • Limited structural data hinders understanding of βMP functions like transport and anchoring.

Purpose of the Study:

  • To develop a computational method for accurate 3D structure prediction of βMPs.
  • To enable genome-wide structural analysis of βMP families.

Main Methods:

  • Predicting strand registers to construct transmembrane domains of βMPs.
  • Utilizing the 3D Beta-barrel Membrane Protein Predictor (3D-BMPP) tool.
  • Modeling extended beta barrels and non-transmembrane loops.

Main Results:

  • Accurate construction of βMP transmembrane domains.
  • High-coverage 3D atomic structure prediction for βMPs.
  • Successful modeling of proteins with limited sequences and novel folds.

Conclusions:

  • 3D-BMPP provides a general and accurate approach for βMP structure prediction.
  • The method facilitates broad applications in understanding βMP functions and genome-wide analysis.