Enhancing the promiscuity of a member of the Caspase protease family by rational design

The N‐terminal cleavage of fusion tags to restore the native N‐terminus of recombinant proteins is a challenging task and up to today, protocols need to be optimized for different proteins individually. Within this work, we present a novel protease that was designed in‐silico to yield enhanced promi...

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Veröffentlicht in:	Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2020-10, Vol.88 (10), p.1303-1318
Hauptverfasser:	Öhlknecht, Christoph, Petrov, Drazen, Engele, Petra, Kröß, Christina, Sprenger, Bernhard, Fischer, Andreas, Lingg, Nico, Schneider, Rainer, Oostenbrink, Chris
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amino acids Amino Acids, Branched-Chain - chemistry Amino Acids, Branched-Chain - metabolism Caspase Caspase 2 - chemistry Caspase 2 - genetics Caspase 2 - metabolism Caspase 3 - chemistry Caspase 3 - genetics Caspase 3 - metabolism Catalytic Domain Cloning, Molecular Cysteine Endopeptidases - chemistry Cysteine Endopeptidases - genetics Cysteine Endopeptidases - metabolism Escherichia coli - genetics Escherichia coli - metabolism free‐energy calculations fusion proteins Gene Expression Genetic Vectors - chemistry Genetic Vectors - metabolism Humans in‐silico modeling Kinetics Molecular Dynamics Simulation molecular simulation Mutants Mutation promiscuity Protease proteases Protein Binding Protein Conformation, alpha-Helical Protein Conformation, beta-Strand Protein Engineering - methods Protein Interaction Domains and Motifs Proteinase Proteins Proteolysis Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Substrate Specificity Thermodynamics
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