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Protein Conformational Disorder and Enzyme Catalysis

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Dynamics in Enzyme Catalysis

Part of the book series: Topics in Current Chemistry ((TOPCURRCHEM,volume 337))

Abstract

Though lacking a well-defined three-dimensional structure, intrinsically unstructured proteins are ubiquitous in nature. These molecules play crucial roles in many cellular processes, especially signaling and regulation. Surprisingly, even enzyme catalysis can tolerate substantial disorder. This observation contravenes conventional wisdom but is relevant to an understanding of how protein dynamics modulates enzyme function. This chapter reviews properties and characteristics of disordered proteins, emphasizing examples of enzymes that lack defined structures, and considers implications of structural disorder for catalytic efficiency and evolution.

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Acknowledgments

The authors are grateful to Dr. An Vandemeulebroucke and Dr. Vladimir Torbeev for fruitful discussions and carefully reading the manuscript and Richard Obexer for refining the figures. Investigations of disordered proteins in the Hilvert group have been generously supported by the Schweizerischer Nationalfonds and the ETH Zürich.

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  1. Laboratory of Organic Chemistry, ETH Zürich, 8093, Zürich, Switzerland

    Cindy Schulenburg & Donald Hilvert

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  1. Cindy Schulenburg
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  2. Donald Hilvert
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Correspondence to Donald Hilvert .

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  1. Department of Chemistry Department of Molecular and Cell Biology, University of California The california institute for Quantitativ, Berkeley, CA, USA

    Judith Klinman

  2. Department of Chemistry, University of Illinois at Urbana-Champai, Urbana, Illinois, USA

    Sharon Hammes- Schiffer

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Schulenburg, C., Hilvert, D. (2013). Protein Conformational Disorder and Enzyme Catalysis. In: Klinman, J., Hammes- Schiffer, S. (eds) Dynamics in Enzyme Catalysis. Topics in Current Chemistry, vol 337. Springer, Berlin, Heidelberg. https://doi.org/10.1007/128_2012_411

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