title: Evolution of protein stability using ribosome display.
abstract: The opportunity to enhance protein stability has a number of potential benefits for biological therapeutics - for example extending in vivo half-life, enabling a longer shelf life, reducing the propensity to aggregate, or enabling soluble expression. Engineering protein stability has been attempted empirically, rationally, and using directed evolution based on phage display. Ribosome display is a powerful in vitro technology for the selection and directed evolution of proteins. Ribosome display is typically used for the generation of high-affinity proteins and peptides. This method extends the utility of ribosome display to selecting for stability, defined as the propensity of a molecule to exist in its folded and active state.
authors.affiliation: Department of Antibody Discovery and Protein Engineering, MedImmune Limited, Cambridge, UK. buchanana@medimmune.com
authors.forename: Andrew
authors.initials: A
authors.lastname: Buchanan
mesh_terms: D019020:Directed Molecular Evolution; D019151:Peptide Library; D015202:Protein Engineering; D017510:Protein Folding; D055550:Protein Stability; D011506:Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D012270:Ribosomes / Q000235:genetics / Q000378:metabolism*
chemical_list: D019151:Peptide Library; D011506:Proteins