Blar i forfatter Artikler, rapporter og annet (kjemi) "Åqvist, Johan Lennart Gösta"

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    • Accurate Computation of Thermodynamic Activation Parameters in the Chorismate Mutase Reaction from Empirical Valence Bond Simulations 

      Wilkins, Ryan Scott; Lund, Bjarte Aarmo; Isaksen, Geir Villy; Åqvist, Johan Lennart Gösta; Brandsdal, Bjørn Olav (Journal article; Tidsskriftartikkel; Peer reviewed, 2023-12-19)
      Chorismate mutase (CM) enzymes have long served as model systems for benchmarking new methods and tools in computational chemistry. Despite the enzymes’ prominence in the literature, the extent of the roles that activation enthalpy and entropy play in catalyzing the conversion of chorismate to prephenate is still subject to debate. Knowledge of these parameters is a key piece in fully understanding ...

    • Computational design of the temperature optimum of an enzyme reaction 

      van der Ent, Florian; Skagseth, Susann; Lund, Bjarte Aarmo; Sočan, Jaka; Griese, Julia J.; Brandsdal, Bjørn Olav; Åqvist, Johan Lennart Gösta (Journal article; Tidsskriftartikkel; Peer reviewed, 2023-06-28)
      Cold-adapted enzymes are characterized both by a higher catalytic activity at low temperatures and by having their temperature optimum down-shifted, compared to mesophilic orthologs. In several cases, the optimum does not coincide with the onset of protein melting but reflects some other type of inactivation. In the psychrophilic α-amylase from an Antarctic bacterium, the inactivation is thought to ...

    • Structure and Mechanism of a Cold-Adapted Bacterial Lipase 

      van der Ent, Florian; Lund, Bjarte Aarmo; Svalberg, Linn; Purg, Miha; Chukwu, Ghislean; Widersten, Mikael; Isaksen, Geir Villy; Brandsdal, Bjørn Olav; Åqvist, Johan Lennart Gösta (Journal article; Tidsskriftartikkel; Peer reviewed, 2022-05-03)
      The structural origin of enzyme cold-adaptation has been the subject of considerable research efforts in recent years. Comparative studies of orthologous mesophilic–psychrophilic enzyme pairs found in nature are an obvious strategy for solving this problem, but they often suffer from relatively low sequence identity of the enzyme pairs. Small bacterial lipases adapted to distinctly different ...

    • Towards Rational Computational Engineering of Psychrophilic Enzymes 

      Socan, Jaka; Isaksen, Geir Villy; Brandsdal, Bjørn Olav; Åqvist, Johan Lennart Gösta (Journal article; Tidsskriftartikkel; Peer reviewed, 2019-12-16)
      Cold-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 ...