Literature DB >> 25676311

Prolyl isomerization and its catalysis in protein folding and protein function.

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.
Copyright © 2015 Elsevier Ltd. All rights reserved.

Entities:  

Keywords:  chaperones; folding enzymes; prolyl isomerases; protein folding; protein regulation

Mesh:

Substances:

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


  21 in total

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Review 10.  Peptidylprolyl Isomerases as In Vivo Carriers for Drugs That Target Various Intracellular Entities.

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