Pinpointing disulfide connectivities in cysteine-rich proteins

Chem Commun (Camb). 2017 Jun 29;53(53):7337-7340. doi: 10.1039/c7cc02333b.

Abstract

A simple MD-based protocol is presented to accurately predict both the sequence and order of disulfide bond formation in proteins containing multiple cysteine residues. It provides a detailed description of their dynamical and structural features, which can be used to perform ensemble-averaged ECD calculations. Plant cyclotides are used as model compounds.

MeSH terms

  • Circular Dichroism
  • Cyclotides / chemistry*
  • Cysteine / chemistry*
  • Disulfides / chemistry*
  • Molecular Dynamics Simulation
  • Thermodynamics
  • Violaceae / chemistry

Substances

  • Cyclotides
  • Disulfides
  • Cysteine