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Isomerase and Chaperone Activity of Prolyl Isomerase in the Folding of Carbonic Anhydrase

Authors: P O, Freskgård; N, Bergenhem; B H, Jonsson; M, Svensson; U, Carlsson;

Isomerase and Chaperone Activity of Prolyl Isomerase in the Folding of Carbonic Anhydrase

Abstract

Several proteins have been discovered that either catalyze slow protein-folding reactions or assist folding in the cell. Prolyl isomerase, which has been shown to accelerate rate-limiting cis-trans peptidyl-proline isomerization steps in the folding pathway, can also participate in the protein-folding process as a chaperone. This function is exerted on an early folding intermediate of carbonic anhydrase, which is thereby prevented from aggregating, whereas the isomerase activity is performed later in the folding process.

Related Organizations
Keywords

Protein Denaturation, Time Factors, Chaperonins, Proline, Proteins, Peptidylprolyl Isomerase, Protein Structure, Tertiary, Humans, Carrier Proteins, Isomerases, Amino Acid Isomerases, Carbonic Anhydrases

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Powered by OpenAIRE graph
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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
206
Top 10%
Top 1%
Top 1%
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