Publication Date:
1992-10-16
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Freskgard, P O -- Bergenhem, N -- Jonsson, B H -- Svensson, M -- Carlsson, U -- New York, N.Y. -- Science. 1992 Oct 16;258(5081):466-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institutionen for Fysik och Matteknik/Department of Chemistry, Linkoping University, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1357751" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Isomerases/*metabolism
;
Carbonic Anhydrases/*ultrastructure
;
Carrier Proteins/*metabolism
;
Chaperonins
;
Humans
;
Isomerases/*metabolism
;
Peptidylprolyl Isomerase
;
Proline/chemistry
;
Protein Denaturation
;
Protein Structure, Tertiary
;
Proteins/*metabolism
;
Time Factors
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
Permalink