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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...
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...
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...
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...
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...
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...

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Related Experiment Video

Updated: May 21, 2026

Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases
22:00

Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases

Published on: November 21, 2010

Deciphering membrane protein structures from protein sequences.

Tilman Flock, A J Venkatakrishnan, K R Vinothkumar

    Genome Biology
    |June 29, 2012
    PubMed
    Summary
    This summary is machine-generated.

    Co-evolving positions in protein sequences provide spatial constraints for a novel computational method. This approach models the structures of membrane proteins, advancing structural biology.

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    Last Updated: May 21, 2026

    Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases
    22:00

    Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases

    Published on: November 21, 2010

    Determining Membrane Protein Topology Using Fluorescence Protease Protection (FPP)
    08:14

    Determining Membrane Protein Topology Using Fluorescence Protease Protection (FPP)

    Published on: April 20, 2015

    From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
    09:55

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

    Published on: July 4, 2016

    Area of Science:

    • Computational biology
    • Structural biology
    • Biophysics

    Background:

    • Membrane proteins are crucial biological components with complex structures.
    • Determining membrane protein structures computationally is challenging due to their hydrophobic nature and dynamic conformations.

    Purpose of the Study:

    • To present a novel computational approach for modeling membrane protein structures.
    • To leverage co-evolving positions in protein sequences as spatial constraints.

    Main Methods:

    • Utilizing co-evolving positions identified from protein sequence alignments.
    • Applying these evolutionary constraints within a computational modeling framework.
    • Developing algorithms to predict three-dimensional structures of membrane proteins.

    Main Results:

    • Successfully modeled membrane protein structures using evolutionary data.
    • Demonstrated the utility of co-evolving positions as effective spatial restraints.
    • The computational approach shows promise for predicting complex protein architectures.

    Conclusions:

    • Co-evolving positions are valuable for computational membrane protein structure prediction.
    • This method offers a new strategy for understanding membrane protein function and design.
    • Further development can enhance the accuracy and applicability of this modeling technique.