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Related Concept Videos

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 Folding01:22

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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...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins
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Regulation of protein function: crystal packing interfaces and conformational dimerization.

Peter B Crowley1, Pedro M Matias, Hualing Mi

  • 1UCD School of Biomolecular and Biomedical Science, Conway Institute, University College Dublin, Belfield, Dublin 4, Ireland. peter.crowley@ucd.ie

Biochemistry
|May 16, 2008
PubMed
Summary

Proteins like plastocyanin may form supramolecular assemblies for efficient electron transport. This study found close protein-protein interactions in crystal structures, suggesting a new mechanism for electron transfer in photosynthesis.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Photosynthesis Research

Background:

  • Interprotein electron transport traditionally involves molecule diffusion.
  • An alternative hypothesis suggests supramolecular protein assemblies facilitate long-range electron transfer.
  • Plastocyanin is a key protein in the photosynthetic electron transport chain.

Purpose of the Study:

  • To investigate crystal packing interfaces of plastocyanin.
  • To assess the potential of these interfaces for in vivo supramolecular assemblies.
  • To explore mechanisms of efficient long-range electron transport.

Main Methods:

  • Analysis of three crystal forms of plastocyanin.
  • Examination of protein-protein interfaces and symmetry-related protein chains.
  • Determination of copper-copper (Cu-Cu) separations.

Main Results:

  • Symmetry-related plastocyanin chains exhibited Cu-Cu separations of less than 25 Angstroms.
  • This close proximity supports efficient electron transfer.
  • One structure revealed two plastocyanin forms with modulated interfaces due to backbone and side chain rearrangements.

Conclusions:

  • Plastocyanin crystal packing suggests potential for in vivo supramolecular assemblies.
  • Close protein proximity in assemblies can facilitate efficient electron transfer.
  • Structural plasticity in plastocyanin allows for modulation of protein-protein interactions.