Synthetic shuffling expands functional protein diversity by allowing amino acids to recombine independently View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2002-12

AUTHORS

Jon E Ness, Seran Kim, Andrea Gottman, Rob Pak, Anke Krebber, Torben V Borchert, Sridhar Govindarajan, Emily C Mundorff, Jeremy Minshull

ABSTRACT

We describe synthetic shuffling, an evolutionary protein engineering technology in which every amino acid from a set of parents is allowed to recombine independently of every other amino acid. With the use of degenerate oligonucleotides, synthetic shuffling provides a direct route from database sequence information to functional libraries. Physical starting genes are unnecessary, and additional design criteria such as optimal codon usage or known beneficial mutations can also be incorporated. We performed synthetic shuffling of 15 subtilisin genes and obtained active and highly chimeric enzymes with desirable combinations of properties that we did not obtain by other directed-evolution methods. More... »

PAGES

1251-1255

Journal

TITLE

Nature Biotechnology

ISSUE

12

VOLUME

20

Author Affiliations

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nbt754

    DOI

    http://dx.doi.org/10.1038/nbt754

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1003186142

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/12426575


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