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Nucleic Acids Research 2005 33(Database Issue):D279-D283; doi:10.1093/nar/gki016
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Nucleic Acids Research, 2005, Vol. 33, Database issue D279-D283
© 2005, the authors
Nucleic Acids Research, Vol. 33, Database issue © Oxford University Press 2005; all rights reserved

PFD: a database for the investigation of protein folding kinetics and stability

Kate F. Fulton1, Glyn L. Devlin1, Rachel A. Jodun1, Linda Silvestri3, Stephen P. Bottomley1, Alan R. Fersht3 and Ashley M. Buckle1,2,*

1 The Department of Biochemistry and Molecular Biology, School of Biomedical Sciences, Faculty of Medicine, 2 Victorian Bioinformatics Consortium, PO Box 53, Monash University, Clayton, Victoria 3800, Australia and 3 Cambridge Centre for Protein Engineering and Cambridge University Chemical Laboratory, MRC Centre, Hills Road, Cambridge, CB2 2QH, UK

* To whom correspondence should be addressed. Tel: +61 3 9905 3781; Fax: +61 3 9905 3781; Email: Ashley.Buckle{at}med.monash.edu.au
Present address: Glyn L. Devlin, Biological Physics Group, Cavendish Laboratory, Cambridge CB3 0HE, UK

Received July 17, 2004; Revised and Accepted September 17, 2004

We have developed a new database that collects all protein folding data into a single, easily accessible public resource. The Protein Folding Database (PFD) contains annotated structural, methodological, kinetic and thermodynamic data for more than 50 proteins, from 39 families. A user-friendly web interface has been developed that allows powerful searching, browsing and information retrieval, whilst providing links to other protein databases. The database structure allows visualization of folding data in a useful and novel way, with a long-term aim of facilitating data mining and bioinformatics approaches. PFD can be accessed freely at http://pfd.med.monash.edu.au.


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K. F. Fulton, M. A. Bate, N. G. Faux, K. Mahmood, C. Betts, and A. M. Buckle
Protein Folding Database (PFD 2.0): an online environment for the International Foldeomics Consortium
Nucleic Acids Res., January 12, 2007; 35(suppl_1): D304 - D307.
[Abstract] [Full Text] [PDF]



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