Journal Article

Reliable prediction of protein thermostability change upon double mutation from amino acid sequence

Liang-Tsung Huang and M. Michael Gromiha

in Bioinformatics

Volume 25, issue 17, pages 2181-2187
Published in print September 2009 | ISSN: 1367-4803
Published online June 2009 | e-ISSN: 1460-2059 | DOI: http://dx.doi.org/10.1093/bioinformatics/btp370
Reliable prediction of protein thermostability change upon double mutation from amino acid sequence

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Summary: The accurate prediction of protein stability change upon mutation is one of the important issues for protein design. In this work, we have focused on the stability change of double mutations and systematically analyzed the wild-type and mutant residues, patterns in amino acid sequence and locations of mutants. Based on the sequence information of wild-type, mutant and three neighboring residues, we have presented a weighted decision table method (WET) for predicting the stability changes of 180 double mutants obtained from thermal (ΔΔG) denaturation. Using 10-fold cross-validation test, our method showed a correlation of 0.75 between experimental and predicted values of stability changes, and an accuracy of 82.2% for discriminating the stabilizing and destabilizing mutants.

Availability: http://bioinformatics.myweb.hinet.net/wetstab.htm

Contact: michael-gromiha@aist.go.jp

Supplementary information: Supplementary data are available at Bioinformatics online.

Journal Article.  4482 words.  Illustrated.

Subjects: Bioinformatics and Computational Biology

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