| Literature DB >> 18573077 |
Christian Jäckel1, Peter Kast, Donald Hilvert.
Abstract
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.Mesh:
Substances:
Year: 2008 PMID: 18573077 DOI: 10.1146/annurev.biophys.37.032807.125832
Source DB: PubMed Journal: Annu Rev Biophys ISSN: 1936-122X Impact factor: 12.981