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Nucleic Acids Research 2006 34(Web Server issue):W70-W74; doi:10.1093/nar/gkl043
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© The Author 2006. Published by Oxford University Press. All rights reserved
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Article

FOLD-RATE: prediction of protein folding rates from amino acid sequence

M. Michael Gromiha*, A. Mary Thangakani1 and S. Selvaraj2

Computational Biology Research Center (CBRC), National Institute of Advanced Industrial Science and Technology (AIST) AIST Tokyo Waterfront Bio-IT Research Building, 2-42 Aomi, Koto-ku, Tokyo 135-0064, Japan 1 Advanced Technology Institute Inc. Tokyo, Japan 2 Department of Bioinformatics, Bharathidasan University Tiruchirappalli 620 024 TN, India

*To whom correspondence should be addressed. Tel: +81 3 3599 8046; Fax: +81 3 3599 8081; Email: michael-gromiha{at}aist.go.jp

Received December 21, 2005. Revised February 3, 2006. Accepted February 3, 2006.

We have developed a web server, FOLD-RATE, for predicting the folding rates of proteins from their amino acid sequences. The relationship between amino acid properties and protein folding rates has been systematically analyzed and a statistical method based on linear regression technique has been proposed for predicting the folding rate of proteins. We found that the classification of proteins into different structural classes shows an excellent correlation between amino acid properties and folding rates of two and three-state proteins. Consequently, different regression equations have been developed for proteins belonging to all-{alpha}, all-ß and mixed class. We observed an excellent agreement between predicted and experimentally observed folding rates of proteins; the correlation coefficients are, 0.99, 0.97 and 0.90, respectively, for all-{alpha}, all-ß and mixed class proteins. The prediction server is freely available at http://psfs.cbrc.jp/fold-rate/.


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