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Folding Cooperativity and the Wrapping of Intermediate States of Soluble Natural Proteins

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Abstract

This chapter focuses on the molecular basis of cooperativity as a means to understand the folding of soluble natural proteins. We explore the concept of protein wrapping, its intimate relation to cooperativity, and its bearing on the expediency of the folding process for natural proteins. As previously described, wrapping refers to the environmental modulation or protection of intramolecular electrostatic interactions through an exclusion of surrounding water that takes place as the chain folds onto itself. Thus, a special many-body picture of the folding process is shown to emerge where the folding chain not only interacts with itself but also shapes the microenvironments that stabilize or destabilize the interactions. This picture reflects a competition between chain folding and backbone hydration leading to the prevalence of backbone hydrogen bonds for natural foldable proteins. A constant of motion governing the folding process emerges from the analysis.

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Authors and Affiliations

  1. Department of Bioengineering, Rice University, E200K George R. Brown Hall, Houston, TX, 77005, USA

    Prof. Dr. Ariel Fernandez (Karl F. Hasselmann Chair in Engineering)

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  1. Prof. Dr. Ariel Fernandez
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Correspondence to Ariel Fernandez .

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© 2010 Springer-Verlag Berlin Heidelberg

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Fernandez, A. (2010). Folding Cooperativity and the Wrapping of Intermediate States of Soluble Natural Proteins. In: Transformative Concepts for Drug Design: Target Wrapping. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-11792-3_3

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  • DOI: https://doi.org/10.1007/978-3-642-11792-3_3

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  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-11791-6

  • Online ISBN: 978-3-642-11792-3

  • eBook Packages: EngineeringEngineering (R0)

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