DSDBASE: a consortium of native and modelled disulphide bonds in proteins

Nucleic Acids Res. 2004 Jan 1;32(Database issue):D200-2. doi: 10.1093/nar/gkh026.

Abstract

DSDBASE is a database of disulphide bonds in proteins, which provides information on native disulphides and those that are stereochemically possible between pairs of residues for all known protein structural entries. The modelling of disulphides has been performed, using MODIP, by the identification of residue pairs that can strainlessly accommodate a covalent cross-link. We also assess the stereochemical quality of the covalent cross-link and grade them appropriately. One of the potential uses of the database is to design site-directed mutants in order to enhance the thermal stability of a protein. The proposed sites of mutations can be viewed specifically with respect to active sites of enzymes and across physiological dimers. The occurrence of native and modelled disulphides increases the dimensions of the database enormously. This database can also be employed for proposing three-dimensional models of disulphide-rich short polypeptides. The database can be accessed from http://www.ncbs.res.in/ approximately faculty/mini/dsdbase/dsdbase.html. Supplementary information can be accessed from http://www.ncbs.res.in/ approximately faculty/mini/dsdbase/nar/suppl.htm.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Computational Biology
  • Databases, Protein*
  • Disulfides / chemistry*
  • Humans
  • Internet
  • Models, Molecular*
  • Mutation
  • Peptides / chemistry
  • Proteins / chemistry*
  • Proteins / genetics
  • Software
  • Structure-Activity Relationship
  • Thermodynamics
  • User-Computer Interface

Substances

  • Disulfides
  • Peptides
  • Proteins