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Showing 1–2 of 2 results
Advanced filters: Author: Miha Purg Clear advanced filters

  • Enzymes from organisms inhabiting cold environments (psychrophiles) have adapted to catalyzing chemical reactions at near freezing temperatures. Here – using molecular dynamics simulations – the authors analyze cold adaptation of psychrophilic α-amylase and provide the structural basis for its low anomalous temperature optimum: the increased mobility of a surface loop involved in substrate interaction.

    • Jaka Sočan
    • Miha Purg
    • Johan Åqvist
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-11

  • Generation and iterative optimization of designed enzymes can provide valuable insights for a more efficient catalysis. Here the authors have followed the iterative improvement of a designed Kemp eliminase and show that remote point mutations could remodel the designed active site via substantial conformational reorganization.

    • Nan-Sook Hong
    • Dušan Petrović
    • Colin J. Jackson
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-10