Beyond binding: using phage display to select for structure, folding and enzymatic activity in proteins

Citation
P. Forrer et al., Beyond binding: using phage display to select for structure, folding and enzymatic activity in proteins, CURR OP STR, 9(4), 1999, pp. 514-520
Citations number
55
Categorie Soggetti
Biochemistry & Biophysics
Journal title
CURRENT OPINION IN STRUCTURAL BIOLOGY
ISSN journal
0959440X → ACNP
Volume
9
Issue
4
Year of publication
1999
Pages
514 - 520
Database
ISI
SICI code
0959-440X(199908)9:4<514:BBUPDT>2.0.ZU;2-X
Abstract
Phage display of a wide range of polypeptides has been increasingly used to identify novel molecules with useful binding properties for research, medi cal and industrial applications. Recent developments include methods for th e selection of stabilized variants of a protein, the selection of regulatab le enzymes and promising strategies for the selection and evolution of prot ein catalysts.