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Showing 1–5 of 5 results
Advanced filters: Author: H. Adrian Bunzel Clear advanced filters

  • Computationally designed enzymes can be substantially improved by directed evolution. Now, it has been shown that evolution can introduce a dynamic network that selectively tightens the transition-state ensemble, giving rise to a negative activation heat capacity. Targeting such transition state conformational dynamics may expedite de novo enzyme creation.

    • H. Adrian Bunzel
    • J. L. Ross Anderson
    • Adrian J. Mulholland
    Research
    Nature Chemistry
    Volume: 13, P: 1017-1022

  • The reasons for epistasis, wherein mutations interact non-additively, are often not fully understood. Now it is found that shifting the rate-limiting step from substrate binding to the chemical reaction step during the directed evolution of β-lactamase correlates with epistasis.

    • Christopher Fröhlich
    • H. Adrian Bunzel
    • Nobuhiko Tokuriki
    ResearchOpen Access
    Nature Catalysis
    Volume: 7, P: 499-509

  • Evolution separates complex modern enzymes from their hypothetical simpler early ancestors, which raises the question of how unevolved sequences can develop new functions. Here a library of non-natural protein sequences was subjected to ultrahigh-throughput screens in microfluidic droplets, leading to the isolation of a phosphodiesterase enzyme capable of hydrolysing the biological second messenger, cyclic AMP.

    • J. David Schnettler
    • Michael S. Wang
    • Michael H. Hecht
    ResearchOpen Access
    Nature Chemistry
    Volume: 16, P: 1200-1208

  • A de novo designed zinc-binding protein has been converted into a highly active, stereoselective catalyst for a hetero-Diels–Alder reaction. Design and directed evolution were used to effectively harness Lewis acid catalysis and create an enzyme more proficient than other reported Diels–Alderases.

    • Sophie Basler
    • Sabine Studer
    • Donald Hilvert
    Research
    Nature Chemistry
    Volume: 13, P: 231-235