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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...
Peptide Bonds02:43

Peptide Bonds

A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
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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Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
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Protein β-interfaces as a generic source of native peptide tectons.

Céline Valéry1, Rishi Pandey, Juliet A Gerrard

  • 1Biomolecular Interaction Centre, University of Canterbury, Private Bag 4800, Christchurch 8140, New Zealand. celine.valery@canterbury.ac.nz

Chemical Communications (Cambridge, England)
|February 28, 2013
PubMed
Summary

Short peptide motifs from protein interfaces self-assemble into reversible nanoarchitectures in water. This discovery offers a new source of peptide building blocks for nanomaterials.

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Area of Science:

  • Biochemistry
  • Materials Science
  • Nanotechnology

Background:

  • Homo-oligomeric proteins feature continuous beta-sheet interfaces.
  • These interfaces mediate protein-protein interactions and assembly.
  • Understanding these interfaces can inform de novo peptide design.

Purpose of the Study:

  • To design self-assembling peptide motifs from protein interfaces.
  • To investigate the self-assembly properties of these designed peptides.
  • To explore the potential of these peptides as building blocks for nanomaterials.

Main Methods:

  • Designed 7-8 amino acid motifs from beta-continuous interfaces of non-related homo-oligomeric proteins.
  • Investigated self-assembly of these peptides in aqueous solutions.
  • Characterized the self-assembled nanoarchitectures and their properties.

Main Results:

  • Designed peptides intrinsically self-assembled into nanoarchitectures in water.
  • The self-assembly process was reversible.
  • The peptides retained properties of their parent protein interfaces.

Conclusions:

  • Identified a novel source of peptide tectons from protein interfaces.
  • Demonstrated the ability of designed peptides to form reversible nanoarchitectures.
  • Opened new avenues for designing peptide-based nanomaterials.