This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1ysb
From Proteopedia
Revision as of 18:40, 29 September 2014 by OCA (Talk | contribs)
1ysb is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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 the sum of their individual effects. The redesigned enzyme induced an increased, temperature-dependent bacterial growth rate under conditions that required its activity, thereby coupling molecular and metabolic engineering.
Computational thermostabilization of an enzyme.,Korkegian A, Black ME, Baker D, Stoddard BL Science. 2005 May 6;308(5723):857-60. PMID:15879217[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Korkegian A, Black ME, Baker D, Stoddard BL. Computational thermostabilization of an enzyme. Science. 2005 May 6;308(5723):857-60. PMID:15879217 doi:308/5723/857