| Literature DB >> 23536241 |
Cindy Schulenburg1, Donald Hilvert.
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.Entities:
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Year: 2013 PMID: 23536241 DOI: 10.1007/128_2012_411
Source DB: PubMed Journal: Top Curr Chem ISSN: 0340-1022