Volsurf computational method applied to the prediction of stability of thermostable enzymes
| Autor: | Andreas Buthe, Paolo Linda, Lucia Gardossi, Cynthia Ebert, Paolo Braiuca |
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| Přispěvatelé: | Braiuca, P, Buthe, A, Ebert, Cynthia, Linda, P, Gardossi, Lucia |
| Rok vydání: | 2007 |
| Předmět: |
Quantitative structure–activity relationship
Hot Temperature Thermostable enzymes Chemistry Protein design Stability (learning theory) Computational Biology General Medicine Models Theoretical Applied Microbiology and Biotechnology Enzymes Protein stability Biochemistry Molecular descriptor Enzyme Stability Regression Analysis Molecular Medicine Databases Protein Biological system Surface protein Hydrophobic and Hydrophilic Interactions Algorithms Thermostability |
| Zdroj: | Biotechnology Journal. 2:214-220 |
| ISSN: | 1860-7314 1860-6768 |
| DOI: | 10.1002/biot.200600175 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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