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Showing 1–8 of 8 results
Advanced filters: Author: Zbynek Prokop Clear advanced filters

  • The identification of aggregation-prone regions in proteins and their suppression through mutations is a powerful strategy to enhance protein solubility and yield, expanding their potential applications. Here, the authors identify miss-annotations on widespread aggregation databases and apply a deep neural network-based predictor that generates a residue-level aggregation profile for protein sequences (AggreProt) to identify aggregation-prone regions in the LinB enzyme and design mutations to suppress aggregation in its exposed regions.

    • Vojtech Cima
    • Antonin Kunka
    • Jan Martinovic
    ResearchOpen Access
    Communications Chemistry
    P: 1-13

  • Renilla luciferase is a popular bioluminescent enzyme, but the molecular details of its mechanism of action on luciferins such as coelenterazine remained elusive. Now, protein crystal structures and biochemical analyses provide an atomistic description of its catalytic mechanism.

    • Andrea Schenkmayerova
    • Martin Toul
    • Martin Marek
    Research
    Nature Catalysis
    Volume: 6, P: 23-38

  • The transplantation of residues from a selective to a nonselective haloalkane dehalogenase yields the correct active site geometry but not function. Computational and biophysical results explain this disparity, showing that the dynamics and hydration of the engineered protein match its parent, not its target.

    • Jan Sykora
    • Jan Brezovsky
    • Jiri Damborsky
    Research
    Nature Chemical Biology
    Volume: 10, P: 428-430

  • NanoLuc luciferase is a popular bioluminescent enzyme, but the molecular details of its mechanism of action on luciferins such as coelenterazine remained elusive. Here the authors use, protein crystal structures and biochemical analyses to provide an atomistic description of its catalytic mechanism and allosteric behaviour.

    • Michal Nemergut
    • Daniel Pluskal
    • Martin Marek
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-20

  • In this work, the authors report a three-step charge-driven coacervation model involving dynamic complexes between a positively charged IDR of human RECQ4 and G-quadruplexes. The IDR also interacts with Replication Protein A, implying RECQ4’s regulatory role.

    • Anna C. Papageorgiou
    • Michaela Pospisilova
    • Konstantinos Tripsianes
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-19

  • Directed evolution commonly relies on point mutations but InDels frequently occur in evolution. Here the authors report a protein-engineering framework based on InDel mutagenesis and fragment transplantation resulting in greater catalysis and longer glow-type bioluminescence of the ancestral luciferase.

    • Andrea Schenkmayerova
    • Gaspar P. Pinto
    • Jiri Damborsky
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-16