Ontology highlight
ABSTRACT:
SUBMITTER: Fortenberry C
PROVIDER: S-EPMC3781211 | biostudies-literature | 2011 Nov
REPOSITORIES: biostudies-literature
Fortenberry Carie C Bowman Elizabeth Anne EA Proffitt Will W Dorr Brent B Combs Steven S Harp Joel J Mizoue Laura L Meiler Jens J
Journal of the American Chemical Society 20111021 45
It has been demonstrated previously that symmetric, homodimeric proteins are energetically favored, which explains their abundance in nature. It has been proposed that such symmetric homodimers underwent gene duplication and fusion to evolve into protein topologies that have a symmetric arrangement of secondary structure elements--"symmetric superfolds". Here, the ROSETTA protein design software was used to computationally engineer a perfectly symmetric variant of imidazole glycerol phosphate sy ...[more]