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Related Concept Videos

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...
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...
Membrane Fluidity01:23

Membrane Fluidity

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.
Membrane Fluidity01:26

Membrane Fluidity

Membrane fluidity is explained by the fluid mosaic model of the cell membrane, which describes the plasma membrane structure as a mosaic of components—including phospholipids, cholesterol, proteins, and carbohydrates—that gives the membrane a fluid character.
Mosaic nature of the membrane
The mosaic characteristic of the membrane helps the plasma membrane remain fluid. The integral proteins and lipids exist as separate but loosely-attached molecules in the membrane. The membrane is a relatively...
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...

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Rapid Assessment of Membrane Protein Quality by Fluorescent Size Exclusion Chromatography
06:26

Rapid Assessment of Membrane Protein Quality by Fluorescent Size Exclusion Chromatography

Published on: January 6, 2023

Membrane proteins can have high kinetic stability.

Robert E Jefferson1, Tracy M Blois, James U Bowie

  • 1Department of Chemistry and Biochemistry, University of California, Los Angeles-Department of Energy Institute for Genomics and Proteomics, Molecular Biology Institute, University of California, Los Angeles , Los Angeles, California 90095, United States.

Journal of the American Chemical Society
|September 17, 2013
PubMed
Summary

Membrane proteins can be kinetically stable, similar to soluble proteins. Diacylglycerol kinase dissociation suggests proteins can remain folded for weeks, impacting biological function and engineering.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Membrane Protein Dynamics

Background:

  • Approximately 10% of soluble proteins exhibit kinetic stability, resisting unfolding for extended periods.
  • The kinetic stability of membrane proteins remains largely unexplored.
  • Understanding membrane protein stability is crucial for their biological function and therapeutic targeting.

Purpose of the Study:

  • To investigate whether membrane proteins can achieve kinetic stability.
  • To determine the unfolding rate of a model membrane protein, diacylglycerol kinase.
  • To assess the implications of kinetic stability for membrane protein evolution and engineering.

Main Methods:

  • Examined the subunit dissociation rate of trimeric diacylglycerol kinase from Escherichia coli.
  • Used dissociation half-life as a proxy for complete protein unfolding.
  • Quantified the timescale of protein conformational changes.

Main Results:

  • Diacylglycerol kinase demonstrated a subunit dissociation half-life of at least several weeks.
  • This indicates that membrane proteins can remain in a stable, folded state for prolonged durations.
  • Kinetic stability is a conserved mechanism across soluble and membrane proteins.

Conclusions:

  • Membrane proteins can exhibit significant kinetic stability, comparable to soluble proteins.
  • Evolution utilizes kinetic stability to regulate membrane protein function.
  • Kinetic stability presents a potential target for future membrane protein engineering endeavors.