Beyond binding: using phage display to select for structure, folding and enzymatic activity in proteins.
Phage display of a wide range of polypeptides has been increasingly used to identify novel molecules with useful binding properties for research, medical and industrial applications. Recent developments include methods for the selection of stabilized variants of a protein, the selection of regulatable enzymes and promising strategies for the selection and evolution of protein catalysts.
Forrer
P
P
Biochemisches Institut, Universität Zürich, Winterthurerstrasse 190, CH-8057, Zürich, Switzerland.
Jung
S
S
Plückthun
A
A
D001435:Bacteriophages / Q000737:chemistry*; D002384:Catalysis; D003001:Cloning, Molecular / Q000379:methods*; D004798:Enzymes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D019151:Peptide Library; D011485:Protein Binding; D015202:Protein Engineering / Q000379:methods*; D017510:Protein Folding; D012641:Selection, Genetic
D004798:Enzymes; D019151:Peptide Library