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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
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...
Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
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Protein Folding01:22

Protein Folding

Overview

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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

Ionic interactions promote transmembrane helix-helix association depending on sequence context.

Jana R Herrmann1, Angelika Fuchs, Johanna C Panitz

  • 1Lehrstuhl für Chemie der Biopolymere, Department für biowissenschaftliche Grundlagen, Technische Universität München, Freising, Germany.

Journal of Molecular Biology
|December 8, 2009
PubMed
Summary
This summary is machine-generated.

Integral membrane protein interactions are driven by transmembrane domains (TMDs). Specific amino acid sequences, including charged and polar residues alongside GxxxG motifs, facilitate both self-interactions and complex charge-based interactions between different TMDs.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Integral membrane protein folding and oligomerization rely on transmembrane helix interactions.
  • Helix-helix interfaces involve specific amino acids and molecular forces.

Purpose of the Study:

  • To investigate the sequence requirements for strong homotypic and heterotypic interactions of transmembrane domains (TMDs).
  • To identify key residues and motifs involved in intramembrane interactions.

Main Methods:

  • Isolation and analysis of strongly self-interacting TMDs from a combinatorial library.
  • Mutational analyses and reconstruction of high-affinity interfaces.
  • Probing heterotypic interactions to identify charge-based interactions.

Main Results:

  • Strongly self-interacting TMDs contain basic, acidic, and polar nonionizable residues, along with C-terminal GxxxG motifs.
  • Cooperation of these residues was confirmed in homotypic interactions.
  • Interhelical charge-charge interactions were observed in heterotypic interactions.
  • Simple motifs of ionizable residues and GxxxG are overrepresented in natural TMDs.
  • Specific combinations of these motifs show high-affinity heterotypic interaction.

Conclusions:

  • Intramembrane charge-charge interactions are sequence-context dependent.
  • These interactions are crucial for both homotypic and heterotypic interactions in many natural TMDs.