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Related Experiment Videos

Vicinal disulfide turns.

Oliviero Carugo1, Masa Cemazar, Sotir Zahariev

  • 1International Centre for Genetic Engineering and Biotechnology, Padriciano 99, 34012 Trieste, Italy.

Protein Engineering
|October 16, 2003
PubMed
Summary

Vicinal disulfide bonds in proteins induce a specific backbone turn, primarily type VIII. This structural constraint suggests vicinal disulfides act as redox-activated conformational switches.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Chemistry

Background:

  • Disulfide bonds are crucial for protein structure and stability.
  • Vicinal disulfides, involving adjacent cysteine residues, are less common but structurally significant.

Purpose of the Study:

  • To investigate the structural consequences of vicinal disulfide bond formation.
  • To determine the conformational changes associated with vicinal disulfides.
  • To explore the potential role of vicinal disulfides as redox switches.

Main Methods:

  • Analysis of protein structures containing vicinal disulfide bonds.
  • Identification and classification of protein backbone turns.
  • Measurement of omega torsion angles.

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Main Results:

  • Vicinal disulfide bond formation is consistently associated with a tight protein backbone turn.
  • Type VIII turns were identified in nearly 90% of analyzed structures.
  • The peptide bond between cysteines exhibits a distorted trans conformation with specific omega torsion angle values.

Conclusions:

  • Vicinal disulfide bonds induce a characteristic structural motif, the type VIII turn.
  • The distinct conformations of oxidized and reduced vicinal disulfides suggest a role as redox-activated conformational switches.