| Literature DB >> 25676311 |
Philipp A M Schmidpeter1, Franz X Schmid2.
Abstract
Prolyl isomerizations are intrinsically slow processes. They determine the rates of many protein folding reactions and control regulatory events in folded proteins. Prolyl isomerases are able to catalyze these isomerizations, and thus, they have the potential to assist protein folding and to modulate protein function. Here, we provide examples for how prolyl isomerizations limit protein folding and are accelerated by prolyl isomerases and how native-state prolyl isomerizations regulate protein functions. The roles of prolines in protein folding and protein function are closely interrelated because both of them depend on the coupling between cis/trans isomerization and conformational changes that can involve extended regions of a protein.Entities:
Keywords: chaperones; folding enzymes; prolyl isomerases; protein folding; protein regulation
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Year: 2015 PMID: 25676311 DOI: 10.1016/j.jmb.2015.01.023
Source DB: PubMed Journal: J Mol Biol ISSN: 0022-2836 Impact factor: 5.469