title: Volsurf computational method applied to the prediction of stability of thermostable enzymes.
abstract: 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.
authors.affiliation: Dipartimento di Scienze Farmaceutiche, Università degli Studi di Trieste, Trieste, Italy. braiuca@units.it
authors.forename: Paolo
authors.initials: P
authors.lastname: Braiuca
authors.forename: Andreas
authors.initials: A
authors.lastname: Buthe
authors.forename: Cynthia
authors.initials: C
authors.lastname: Ebert
authors.forename: Paolo
authors.initials: P
authors.lastname: Linda
authors.forename: Lucia
authors.initials: L
authors.lastname: Gardossi
mesh_terms: D000465:Algorithms; D019295:Computational Biology / Q000379:methods*; D030562:Databases, Protein; D004795:Enzyme Stability; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism*; D006358:Hot Temperature; D057927:Hydrophobic and Hydrophilic Interactions; D008962:Models, Theoretical; D012044:Regression Analysis
chemical_list: D004798:Enzymes