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Isomerase and chaperone activity of prolyl isomerase in the folding of carbonic anhydrase.

作者信息

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

机构信息

Institutionen för Fysik och Mätteknik/Department of Chemistry, Linköping University, Sweden.

出版信息

Science. 1992 Oct 16;258(5081):466-8. doi: 10.1126/science.1357751.

DOI:10.1126/science.1357751
PMID:1357751
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.

摘要

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