Protein Design by Directed Evolution

@article{citeulike:2770243, 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.}, author = {Jackel, Christian and Kast, Peter and Hilvert, Donald }, citeulike-article-id = {2770243}, doi = {10.1146/annurev.biophys.37.032807.125832}, journal = {Annual Review of Biophysics}, keywords = {protein\_design, review, synthetic\_biology}, number = {1}, pages = {153--173}, posted-at = {2008-06-25 08:26:36}, priority = {2}, title = {Protein Design by Directed Evolution}, url = {http://arjournals.annualreviews.org/doi/abs/10.1146/annurev.biophys.37.032807.125832}, volume = {37}, year = {2008} }

TY - JOUR ID - citeulike:2770243 L3 - citeulike-article-id:2770243 TI - Protein Design by Directed Evolution JF - Annual Review of Biophysics VL - 37 IS - 1 SP - 153 EP - 173 N2 - 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. KW - protein_design KW - review KW - synthetic_biology AU - Jackel, Christian AU - Kast, Peter AU - Hilvert, Donald PY - 2008/// UR - http://arjournals.annualreviews.org/doi/abs/10.1146/annurev.biophys.37.032807.125832 ER -