title: Prolyl isomerization and its catalysis in protein folding and protein function.
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.
authors: Laboratorium für Biochemie und Bayreuther Zentrum für Molekulare Biologie, Universität Bayreuth, 95440 Bayreuth, Germany.
authors: Philipp A M
authors: PA
authors: Schmidpeter
authors: Laboratorium für Biochemie und Bayreuther Zentrum für Molekulare Biologie, Universität Bayreuth, 95440 Bayreuth, Germany. Electronic address: fx.schmid@uni-bayreuth.de.
authors: Franz X
authors: FX
authors: Schmid
mesh_terms: D000818:Animals; D002384:Catalysis; D006801:Humans; D008958:Models, Molecular; D019696:Peptidylprolyl Isomerase / Q000378:metabolism*; D017510:Protein Folding; D011499:Protein Processing, Post-Translational; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000378:metabolism / Q000502:physiology*
chemical_list: D011506:Proteins; D019696:Peptidylprolyl Isomerase
keywords: chaperones; folding enzymes; prolyl isomerases; protein folding; protein regulation