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Related Concept Videos

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...
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...
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...
Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
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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Purification of the Sarco-Endoplasmic Reticulum Ca2+-ATPase from Rabbit Muscle
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Membrane proteins: from bench to bits.

Gunnar von Heijne1

  • 1Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, Sweden. gunnar@dbb.su.se

Biochemical Society Transactions
|May 24, 2011
PubMed
Summary
This summary is machine-generated.

Recent studies reveal membrane proteins are more flexible and less hydrophobic than previously thought. This complexity challenges current understanding of protein insertion and folding within cell membranes.

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Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • High-resolution X-ray structures have advanced membrane protein research.
  • Initial structures revealed tightly packed, hydrophobic transmembrane alpha-helices.
  • Emerging data shows greater diversity in membrane protein structures.

Purpose of the Study:

  • To explore the evolving understanding of membrane protein structure and flexibility.
  • To address the implications of structural diversity on protein biogenesis.
  • To highlight challenges in predicting membrane protein topology and structure.

Main Methods:

  • Analysis of high-resolution X-ray crystallographic data.
  • Comparative structural analysis of diverse membrane proteins.
  • Bioinformatic approaches for topology and structure prediction.

Main Results:

  • Membrane proteins exhibit significant flexibility.
  • Transmembrane segments can be non-hydrophobic and non-helical.
  • Structural diversity challenges previous models.

Conclusions:

  • The in vivo insertion and folding mechanisms of membrane proteins require re-evaluation.
  • Predictive bioinformatics models need to account for increased structural plasticity.
  • Further research is needed to fully understand membrane protein biogenesis.