title: Engineering proteins for thermostability: the use of sequence alignments versus rational design and directed evolution.
abstract: With the advent of directed evolution techniques, protein engineering has received a fresh impetus. Engineering proteins for thermostability is a particularly exciting and challenging field, as it is crucial for broadening the industrial use of recombinant proteins. In addition to directed evolution, a variety of partially successful rational concepts for engineering thermostability have been developed in the past. Recent results suggest that amino acid sequence comparisons of mesophilic proteins alone can be used efficiently to engineer thermostable proteins. The potential benefits of the underlying, semirational 'consensus concept' are compared with those of rational design and directed evolution approaches.
authors.affiliation: F Hoffmann-La Roche Ltd., Vitamins and Fine Chemicals Division, Department VFB, Building 203, CH-4070 Basel, Switzerland. martin.lehman@roche.com
authors.forename: M
authors.initials: M
authors.lastname: Lehmann
authors.forename: M
authors.initials: M
authors.lastname: Wyss
mesh_terms: D019020:Directed Molecular Evolution / Q000379:methods*; D015195:Drug Design; D004355:Drug Stability; D006358:Hot Temperature; D015202:Protein Engineering / Q000379:methods; D011994:Recombinant Proteins / Q000235:genetics* / Q000627:therapeutic use*; D016415:Sequence Alignment / Q000379:methods*
chemical_list: D011994:Recombinant Proteins