Analysis of factors that induce cysteine bonding state

Comput Biol Med. 2009 Apr;39(4):332-9. doi: 10.1016/j.compbiomed.2009.01.006. Epub 2009 Feb 25.

Abstract

Regarding the fact that the protein structure is principally encoded in its sequence, investigating the bonding state of cysteine has gained a great deal of attention due to its significance in the formation of protein structure. Due to lack of evident influence of free cysteines on the protein structure, it may be expected that only half-cystines convey encoded information. The results obtained from the analysis of amino acid distribution in proximity of both states of cysteines explicitly indicated that perquisite information for inducing cysteine bonding state is present even in the flanking amino acid sequences of free cysteines.

MeSH terms

  • Amino Acids / chemistry
  • Computational Biology / methods*
  • Computer Simulation
  • Cysteine / chemistry*
  • Databases, Protein
  • Disulfides
  • Molecular Conformation
  • Molecular Structure
  • Protein Folding
  • Protein Structure, Tertiary
  • Proteins / chemistry
  • Sequence Analysis, Protein
  • Software

Substances

  • Amino Acids
  • Disulfides
  • Proteins
  • Cysteine