Systematic Optimization of Interface Interactions Increases the Thermostability of a Multimeric Enzyme

Abstract

Stapling subunits: The limited stability of multimers (see picture) is often associated with subunit dissociation. A novel procedure was applied on the basis of crystal structure analysis, sequence alignment, and single-site saturation mutagenesis to systematically identify residues in the inter-subunit interface suitable for increasing stability. As a service to our authors and readers, this journal provides supporting information supplied by the authors. Such materials are peer reviewed and may be re-organized for online delivery, but are not copy-edited or typeset. Technical support issues arising from supporting information (other than missing files) should be addressed to the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.