Analycys: a database for conservation and conformation of disulphide bonds in homologous protein domains

Proteins. 2007 May 1;67(2):255-61. doi: 10.1002/prot.21318.


Disulphide bonds in proteins are known to play diverse roles ranging from folding to structure to function. Thorough knowledge of the conservation status and structural state of the disulphide bonds will help in understanding of the differences in homologous proteins. Here we present a database for the analysis of conservation and conformation of disulphide bonds in SCOP structural families. This database has a wide range of applications including mapping of disulphide bond mutation patterns, identification of disulphide bonds important for folding and stabilization, modeling of protein tertiary structures and in protein engineering. The database can be accessed at:

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Conserved Sequence
  • Databases, Protein*
  • Disulfides / chemistry*
  • Internet
  • Mutation
  • Protein Conformation
  • Proteins / chemistry*
  • Proteins / physiology
  • Structural Homology, Protein*


  • Disulfides
  • Proteins