Ontology highlight
ABSTRACT:
SUBMITTER: Korkegian A
PROVIDER: S-EPMC3412875 | biostudies-literature | 2005 May
REPOSITORIES: biostudies-literature
Korkegian Aaron A Black Margaret E ME Baker David D Stoddard Barry L BL
Science (New York, N.Y.) 20050501 5723
Thermostabilizing an enzyme while maintaining its activity for industrial or biomedical applications can be difficult with traditional selection methods. We describe a rapid computational approach that identified three mutations within a model enzyme that produced a 10 degrees C increase in apparent melting temperature T(m) and a 30-fold increase in half-life at 50 degrees C, with no reduction in catalytic efficiency. The effects of the mutations were synergistic, giving an increase in excess of ...[more]