Protein Design by Directed Evolution
- 1 June 2008
- journal article
- review article
- Published by Annual Reviews in Annual Review of Biophysics
- Vol. 37 (1), 153-173
- https://doi.org/10.1146/annurev.biophys.37.032807.125832
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.Keywords
This publication has 86 references indexed in Scilit:
- A simple selection strategy for evolving highly efficient enzymesNature Biotechnology, 2007
- Metabolic engineering of a genetic selection system with tunable stringencyProceedings of the National Academy of Sciences of the United States of America, 2007
- New algorithms and an in silico benchmark for computational enzyme designProtein Science, 2006
- 1.6Å Crystal Structure of the Secreted Chorismate Mutase from Mycobacterium tuberculosis: Novel Fold Topology RevealedJournal of Molecular Biology, 2006
- Intrinsically unstructured proteins and their functionsNature Reviews Molecular Cell Biology, 2005
- Energy Functions for Protein Design: Adjustment with Protein–Protein Complex Affinities, Models for the Unfolded State, and Negative Design of Solubility and SpecificityJournal of Molecular Biology, 2005
- A novel ADP- and zinc-binding fold from function-directed in vitro evolutionNature Structural & Molecular Biology, 2004
- Evolutionarily conserved networks of residues mediate allosteric communication in proteinsNature Structural & Molecular Biology, 2002
- Generalized dead-end elimination algorithms make large-scale protein side-chain structure prediction tractable: implications for protein design and structural genomicsJournal of Molecular Biology, 2001
- High-Resolution Protein Design with Backbone FreedomScience, 1998