title: Systematic optimization of interface interactions increases the thermostability of a multimeric enzyme.
authors.affiliation: Bioprocess Laboratory, Department of Biosystems Science and Engineering, ETH Zurich, Mattenstrasse 26, 4058 Basel, Switzerland.
authors.forename: Andreas
authors.initials: A
authors.lastname: Bosshart
authors.forename: Sven
authors.initials: S
authors.lastname: Panke
authors.forename: Matthias
authors.initials: M
authors.lastname: Bechtold
mesh_terms: D002238:Carbohydrate Epimerases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism; D016297:Mutagenesis, Site-Directed; D015202:Protein Engineering; D054730:Protein Interaction Domains and Motifs; D055550:Protein Stability; D017434:Protein Structure, Tertiary; D011549:Pseudomonas / Q000201:enzymology; D013696:Temperature
chemical_list: D002238:Carbohydrate Epimerases; C525624:D-tagatose 3-epimerase, Pseudomonas cichorii
keywords: carbohydrates; enzymatic catalysis; isomerases; protein engineering; protein stability