Systematic optimization of interface interactions increases the thermostability of a multimeric enzyme

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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. Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

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Bosshart, A., Panke, S., & Bechtold, M. (2013). Systematic optimization of interface interactions increases the thermostability of a multimeric enzyme. Angewandte Chemie - International Edition, 52(37), 9673–9676. https://doi.org/10.1002/anie.201304141

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