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dc.contributor.authorSocan, Jaka
dc.contributor.authorIsaksen, Geir Villy
dc.contributor.authorBrandsdal, Bjørn Olav
dc.contributor.authorÅqvist, Johan Lennart Gösta
dc.date.accessioned2020-02-27T11:33:08Z
dc.date.available2020-02-27T11:33:08Z
dc.date.issued2019-12-16
dc.description.abstractCold-adapted enzymes from psychrophilic species achieve their high catalytic efficiency at low temperature by a different partitioning of the activation free energy into its enthalpic and entropic components, compared to orthologous mesophilic enzymes. Their lower activation enthalpy, partly compensated by an increased entropic penalty, has been suggested to originate from changes in flexibility of the protein surface. Multiple sequence alignments of psychrophilic and mesophilic enzymes also show characteristic motifs located in surface loops of the protein. Here, we use computer simulations to examine the effects of a number of designed surface mutations of psychrophilic and mesophilic elastases on the temperature dependence of the catalyzed peptide cleavage reaction. For each of 14 mutant enzyme variants we report calculations of their thermodynamic activation parameters. The results show that substitution of psychrophilic loop residues into the mesophilic enzyme consistently changes both the activation parameters and loop flexibilities towards the former, and vice versa for opposite substitutions.en_US
dc.identifier.citationSocan J, Isaksen GVI, Brandsdal BO, Åqvist JLG. Towards Rational Computational Engineering of Psychrophilic Enzymes. Scientific Reports. 2019;9(19147)en_US
dc.identifier.cristinIDFRIDAID 1763039
dc.identifier.doi10.1038/s41598-019-55697-4
dc.identifier.issn2045-2322
dc.identifier.urihttps://hdl.handle.net/10037/17530
dc.language.isoengen_US
dc.publisherNature Researchen_US
dc.relation.journalScientific Reports
dc.relation.projectIDNorges forskningsråd: 262695en_US
dc.relation.projectIDNorges forskningsråd: 274858en_US
dc.relation.projectIDinfo:eu-repo/grantAgreement/RCN/SFF/262695/Norway/Hylleraas Centre for Quantum Molecular Sciences//en_US
dc.relation.projectIDinfo:eu-repo/grantAgreement/RCN/FRINATEK/274858/Norway/Evolutionary Principles of Biocatalysts From Extreme Environments//en_US
dc.rights.accessRightsopenAccessen_US
dc.rights.holderCopyright 2019 The Author(s)en_US
dc.subjectVDP::Mathematics and natural science: 400en_US
dc.subjectVDP::Matematikk og Naturvitenskap: 400en_US
dc.titleTowards Rational Computational Engineering of Psychrophilic Enzymesen_US
dc.type.versionpublishedVersionen_US
dc.typeJournal articleen_US
dc.typeTidsskriftartikkelen_US
dc.typePeer revieweden_US


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