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Protein Stabilization by the Rational Design of Surface Charge–Charge Interactions

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Protein Structure, Stability, and Interactions

Part of the book series: Methods in Molecular Biology ((MIMB,volume 490))

Abstract

The design of proteins with increased stability has many important applications in biotechnology. In recent years, strategies involving directed evolution, sequence-based design, or computational design have proven successful for generating stabilized proteins. A brief overview of the various methods that have been used to increase protein stability is presented, followed by a detailed example of how the rational design of surface charge–charge interactions has provided a robust method for protein stabilization.

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Acknowledgements

The work on optimization of charge–charge interactions in proteins is supported by a grant from the National Science Foundation (MCB 0416746 to G.I.M.). K.L.S. is a recipient of NASA Graduate Student Researchers Program Fellowship.

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  1. Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, USA

    Katrina L. Schweiker & George I. Makhatadze

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  1. Katrina L. Schweiker
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    © 2009 Humana Press, a part of Springer Science+Business Media, LLC

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    Schweiker, K.L., Makhatadze, G.I. (2009). Protein Stabilization by the Rational Design of Surface Charge–Charge Interactions. In: Shriver, J. (eds) Protein Structure, Stability, and Interactions. Methods in Molecular Biology, vol 490. Humana Press. https://doi.org/10.1007/978-1-59745-367-7_11

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