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PMID: 1731198 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Protein folding in the cell.

Nature ·Vol. 355 ·No. 6355 ·1992-01-02 ·Pages 33-45

Gething MJ, Sambrook J

Abstract

In the cell, as in vitro, the final conformation of a protein is determined by its amino-acid sequence. But whereas some isolated proteins can be denatured and refolded in vitro in the absence of other macromolecular cellular components, folding and assembly of polypeptides in vivo involves other proteins, many of which belong to families that have been highly conserved during evolution.

MeSH Terms

Amino Acid Isomerases/metabolism Amino Acid Sequence Animals Carrier Proteins/metabolism Cell Physiological Phenomena Heat-Shock Proteins/metabolism Isomerases/metabolism Models, Molecular Molecular Sequence Data Peptidylprolyl Isomerase Protein Conformation Protein Disulfide-Isomerases Proteins/metabolism Thioredoxins/metabolism

Chemicals

Carrier Proteins Heat-Shock Proteins Proteins Thioredoxins Isomerases Amino Acid Isomerases Peptidylprolyl Isomerase Protein Disulfide-Isomerases

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Gething M J

Department of Biochemistry, University of Texas Southwestern Medical Centre, Dallas 75235.

Sambrook J

Article Info

Journal

Nature

Abbr.

Nature

ISSN

0028-0836

DOI

10.1038/355033a0

Published

1992-01-02

Pages

33-45

Language

English

Region

England

NLM ID

0410462

Subset

External Links

PubMed source DOI: 10.1038/355033a0 View journal details

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Protein folding in the cell.

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