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PMID: 3378031 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Folding of the nascent peptide chain into a biologically active protein.

Biochemistry ·Vol. 27 ·No. 6 ·1988-03-22 ·Pages 1809-12

Tsou CL

Abstract

The refolding of denatured proteins with complete sequences may not be fast enough to account for the in vivo folding of growing peptide chains during biosynthesis. As some peptide fragments have secondary structures not unlike those of the corresponding segments in the intact molecules and native disulfide bonds of some proteins can form cotranslationally, it is suggested that the folding of the nascent chain begins early during synthesis. However, further adjustments may be necessary during chain elongation and after posttranslational modifications of the completed peptide chain to generate the native conformation of a biologically active protein.

MeSH Terms
Circular Dichroism Models, Biological Peptides Protein Conformation Protein Denaturation Protein Processing, Post-Translational Proteins/genetics
Chemicals
Peptides Proteins
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Tsou C L
Laboratory of Molecular Enzymology, Academia Sinica, Beijing, China.
Article Info
Journal
Biochemistry
Abbr.
Biochemistry
ISSN
0006-2960
Published
1988-03-22
Pages
1809-12
Language
English
Region
United States
NLM ID
0370623
Subset
IM
Grants
NIDDK NIH HHS · R01 DK 34035 · United States
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