Prolyl Isomerization and Its Catalysis in Protein Folding and Protein Function

• Prolyl isomerizations control the folding and regulate the function of proteins.
• In both cases, cis/trans isomerization couples with conformational folding reactions.
• Prolyl isomerization can provide allosteric proteins with a molecular memory.
• Chaperone domains boost the catalysis of protein folding by prolyl isomerases.

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.

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