title: Control of protein function by prolyl isomerization.
abstract: BACKGROUND
  Prolyl cis/trans isomerizations have long been known as critical and rate-limiting steps in protein folding.
  
  
  RESULTS
  Now it is clear that they are also used as slow conformational switches and molecular timers in the regulation of protein activity. Here we describe several such proline switches and how they are regulated.
  
  
  CONCLUSIONS
  Prolyl isomerizations can function as attenuators and provide allosteric systems with a molecular memory. This article is part of a Special Issue entitled Proline-directed Foldases: Cell Signaling Catalysts and Drug Targets.
authors.affiliation: Laboratorium für Biochemie und Bayreuther Zentrum für Molekulare Biowissenschaften, Universität Bayreuth, 95440 Bayreuth, Germany.
authors.forename: Philipp A M
authors.initials: PA
authors.lastname: Schmidpeter
authors.affiliation: Laboratorium für Biochemie und Bayreuther Zentrum für Molekulare Biowissenschaften, Universität Bayreuth, 95440 Bayreuth, Germany.
authors.forename: Johanna R
authors.initials: JR
authors.lastname: Koch
authors.affiliation: Laboratorium für Biochemie und Bayreuther Zentrum für Molekulare Biowissenschaften, Universität Bayreuth, 95440 Bayreuth, Germany. Electronic address: fx.schmid@uni-bayreuth.de.
authors.forename: Franz X
authors.initials: FX
authors.lastname: Schmid
mesh_terms: D000494:Allosteric Regulation / Q000502:physiology; D000818:Animals; D006801:Humans; D011392:Proline / Q000737:chemistry* / Q000378:metabolism; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D011506:Proteins; D011392:Proline
keywords: Allostery; Prolyl isomerase; Protein folding; Protein regulation; Signaling