Journal
ANNUAL REVIEW OF BIOPHYSICS
Volume 37, Issue -, Pages 153-173Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev.biophys.37.032807.125832
Keywords
molecular diversity; random mutagenesis; screening; selection; enzymes; computational design
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While nature evolved polypeptides over billions of years, protein design by evolutionary mimicry is progressing at a far more rapid pace. The mutation, selection, and amplification steps of the evolutionary cycle may be imitated in the laboratory using existing proteins, or molecules created de novo from random sequence space, as starting templates. However, the astronomically large number of possible polypeptide sequences remains an obstacle to identifying and isolating functionally interesting variants. Intelligently designed libraries and improved search techniques are consequently important for future advances. In this regard, combining experimental and computational methods holds particular promise for the creation of tailored protein receptors and catalysts for tasks unimagined by nature.
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