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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
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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...
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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 types have...
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Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
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Published on: March 5, 2017

Helix-packing motifs in membrane proteins.

R F S Walters1, W F DeGrado

  • 1Department of Biochemistry and Biophysics and Chemistry, University of Pennsylvania, Philadelphia, PA 19104-6059, USA.

Proceedings of the National Academy of Sciences of the United States of America
|September 7, 2006
PubMed
Summary

Researchers identified five common transmembrane helix-packing motifs in proteins. These structural and sequence patterns simplify membrane protein design and prediction.

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Area of Science:

  • Structural Biology
  • Biochemistry
  • Computational Biology

Background:

  • Membrane protein structure is crucial for function.
  • Interactions between transmembrane helices dictate protein folding.
  • Understanding these interactions is key to predicting protein structures.

Purpose of the Study:

  • To identify and classify recurring helix-helix interaction motifs in membrane proteins.
  • To simplify the complex universe of transmembrane helix-pairing.
  • To provide insights for membrane protein design and structural prediction.

Main Methods:

  • Dissecting crystallographic structures of membrane proteins into helical pairs.
  • Clustering pairs based on three-dimensional similarity (RMSD <= 1.5 Å).
  • Analyzing structural features and sequence propensities of common motifs.

Main Results:

  • 90% of helical pairs assigned to clusters of at least five members.
  • Three-quarters of pairs belong to five tightly clustered motifs.
  • Identified common packing principles, including residue segregation patterns for parallel and antiparallel helices.

Conclusions:

  • The common transmembrane helix-pairing motifs are surprisingly simple and limited.
  • Derived position-specific sequence propensities for key motifs.
  • These findings offer valuable tools for designing and predicting membrane protein structures.