Nuclc. Acids. Res. OUP
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DSDBASE

http://www.ncbs.res.in/%7Efaculty/mini/dsdbase/dsdbase.html

Vinayagam, A., Sowdhamini, R.

National Centre for Biological Sciences UAS-GKVK campus Bellary Road Bangalore 560 065 INDIA

Contact   mini@ncbs.res.in


Database Description

A database of disulphide bonds in proteins (DSDBASE) has been developed that provides information on native disulphides and also those disulphides which are stereochemically possible between pairs of residues in a protein. The modelling of disulphides has been performed using the program MODIP. And has been applied to 1131 non-redundant protein chains giving rise to 47518 possible disulphide bond positions. We also assess the stereochemical quality of the covalent cross-link and grade them appropriately. For every protein considered in our database, we provide a list of possible sites where disulphides could be introduced along with their stereochemical grades. The occurrence of native and modelled disulphides increases the dimensions of the database enormously. One of the potential uses of such a disulphide database is to design site-directed mutants in order to enhance the thermal stability of the protein in question. This database can also be employed for proposing three-dimensional models of disulphide-rich polypeptides like toxins and small proteins. The database is accessible from http://www.ncbs.res.in/%7Efaculty/mini/dsdbase/dsdbase.html

Acknowledgements

This work is supported by a Senior Research Fellowship from Wellcome Trust awarded to RS.

REFERENCES

  1. R.Sowdhamini, N.Srinivasan, B.Shoichet, D.V.Santi, C.Ramakrishnan & P.Balaram (1989). Stereochemical modelling of disulfide bridges: Criteria for introduction into proteins by site-directed mutagenesis. Prot. Engng., 3, 95-103.

Category   Structure

 

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