Article
Effect of multiple symmetries on the association of R67 DHFR subunits bearing interfacial complementing mutations.
Protein science : a publication of the Protein Society - 1 Jan 2004
Dam Julie, Blondel Arnaud
Abstract excerpt
It was shown previously that complementation could be a powerful mean to probe protein-protein interactions in the normally tetrameric R67 DHFR. Indeed, mixing complementing inactive dimeric mutants produced active heterotetramers. This approach turned a homo-oligomer into a hetero-oligomer and thus allowed the use of combinatorial assays, a subtle analysis of the association forces, and a precise determination...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
