Iterative saturation mutagenesis: A powerful approach to engineer proteins by systematically simulating darwinian evolution

Methods in Molecular Biology

Volumn 1179, Issue , 2014, Pages 103-128

  Acevedo Rocha, Carlos G ^a,b   Hoebenreich, Sabrina ^a   Reetz, Manfred T ^a,b  

^a PHILIPPS UNIVERSITY MARBURG   (Germany)

^b MAX PLANCK INSTITUT FÜR KOHLENFORSCHUNG   (Germany)

Author keywords

B FIT; CAST; Directed evolution; Library quality; Library statistics; P450 BM3; Protein engineering; Saturation mutagenesis; Screening effort; Steroids

Indexed keywords

AMINO ACID; CYTOCHROME P450 BM3; TESTOSTERONE;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; BIOCATALYSIS; BIOCATALYST; CODON; ENZYME ACTIVE SITE; ENZYME ACTIVITY; EPISTASIS; GENE AMPLIFICATION; GENE LIBRARY; GENETIC SCREENING; GENETIC SELECTION; GENETIC VARIABILITY; IN VITRO STUDY; ITERATIVE SATURATION MUTAGENESIS; MOLECULAR DOCKING; MOLECULAR EVOLUTION; MUTAGENESIS; NONHUMAN; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN ENGINEERING; PROTEIN STRUCTURE; SIMULATION; THERMOSTABILITY; CHEMICAL STRUCTURE; DIRECTED MOLECULAR EVOLUTION; GENETICS;

DIRECTED MOLECULAR EVOLUTION; GENE LIBRARY; MODELS, MOLECULAR; MUTAGENESIS;

EID: 84925883245     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4939-1053-3_7     Document Type: Article

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