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Volsurf computational method applied to the prediction of stability of thermostable enzymes
Author(s) -
Braiuca Paolo,
Buthe Andreas,
Ebert Cynthia,
Linda Paolo,
Gardossi Lucia
Publication year - 2007
Publication title -
biotechnology journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.144
H-Index - 84
eISSN - 1860-7314
pISSN - 1860-6768
DOI - 10.1002/biot.200600175
Subject(s) - thermostability , stability (learning theory) , protein stability , computer science , protein design , multivariate statistics , protein engineering , basis (linear algebra) , biological system , thermophile , macromolecule , protein structure prediction , biochemical engineering , computational biology , protein structure , chemistry , mathematics , machine learning , enzyme , biology , biochemistry , engineering , geometry
A computational model for the quantitative prediction of protein thermostability has been developed by means of the Volsurf method. A data set of 22 enzymes of reported thermostability in water systems, for the most part coming from thermophilic and hyperthermophilic organisms, has been built up. Molecular descriptors of the protein surface have been calculated and their role in the stabilization of the macromolecule has been analyzed by a multivariate statistical approach. The resulting regression model has shown a good predictivity and it has been able to quantitatively identify some structural requirements correlated with protein stability. The method can be the basis for a new computational support tool in rational protein design, which is complementary to the existing methods based on the sequence analysis.