title: Engineering aggregation-resistant proteins by directed evolution.
abstract: A method was recently described for selecting aggregation-resistant antibody domains. A repertoire of domains displayed on filamentous bacteriophage were heated/cooled and selected for binding to the affinity ligand protein A specific for the folded domains. Here we describe a generalization of the method based on the selection for retained phage infectivity and for the binding of an appended sequence tag, and applicable to any protein displayable in multivalent form on phage.
authors.affiliation: Centre for Protein Engineering, Medical Research Council Centre, Cambridge, UK.
authors.forename: K
authors.initials: K
authors.lastname: Famm
authors.forename: G
authors.initials: G
authors.lastname: Winter
mesh_terms: D019143:Evolution, Molecular; D005821:Genetic Techniques; D008024:Ligands; D046529:Microscopy, Electron, Transmission; D016296:Mutagenesis; D019151:Peptide Library; D011485:Protein Binding; D015202:Protein Engineering / Q000379:methods*; D017434:Protein Structure, Tertiary; D013997:Time Factors
chemical_list: D008024:Ligands; D019151:Peptide Library