Prolyl isomerization and its catalysis in protein folding and protein function. Review uri icon

Overview

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.

publication date

  • February 9, 2015

Research

keywords

  • Peptidylprolyl Isomerase
  • Protein Folding
  • Protein Processing, Post-Translational
  • Proteins

Identity

Scopus Document Identifier

  • 84924226961

Digital Object Identifier (DOI)

  • 10.1016/j.jmb.2015.01.023

PubMed ID

  • 25676311

Additional Document Info

volume

  • 427

issue

  • 7