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Erschienen in:
Relationship of Femtosecond–Picosecond Dynamics to Enzyme-Catalyzed H-Transfer Kapitel lesen Erstes Kapitel lesen

2013 | OriginalPaper | Buchkapitel

Protein Conformational Disorder and Enzyme Catalysis

verfasst von : Cindy Schulenburg, Donald Hilvert

Erschienen in: Dynamics in Enzyme Catalysis

Verlag: Springer Berlin Heidelberg

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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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Vorheriges Kapitel Relationship of Femtosecond–Picosecond Dynamics to Enzyme-Catalyzed H-Transfer
Nächstes Kapitel A Surprising Role for Conformational Entropy in Protein Function
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Metadaten
Titel
Protein Conformational Disorder and Enzyme Catalysis
verfasst von
Cindy Schulenburg
Donald Hilvert
Copyright-Jahr
2013
Verlag
Springer Berlin Heidelberg
Buch
Dynamics in Enzyme Catalysis

Print ISBN: 978-3-642-38961-0

Electronic ISBN: 978-3-642-38962-7

Copyright-Jahr: 2013

DOI
https://doi.org/10.1007/128_2012_411

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