Ironing out the protein folding problem?

Folding an isolated or expressed globular protein is a major biotechnological problem and often limits the commercialization of protein-based therapeutics. In this issue, Alan Fersht and colleagues present a potential solution, using a biomimetic approach that exploits elements of the cellular machi...

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Bibliographic Details
Published in:Nature biotechnology 1999-02, Vol.17 (2), p.136-137
Main Author: Horowitz, Paul M
Format: Article
Language:English
Subjects:
Agriculture
Bioinformatics
Biomedical and Life Sciences
Biomedical Engineering/Biotechnology
Biomedicine
Biotechnology
Chaperonin 60 - metabolism
Life Sciences
Protein Folding
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Summary:Folding an isolated or expressed globular protein is a major biotechnological problem and often limits the commercialization of protein-based therapeutics. In this issue, Alan Fersht and colleagues present a potential solution, using a biomimetic approach that exploits elements of the cellular machinery to fold proteins in vitro. Their work involves the application of several immobilized reagents that are designed to prevent aggregation and avoid kinetic traps of incorrect disulfide pairing and/or incorrect isomers of peptide bonds involving proline.
ISSN:1087-0156
1546-1696
DOI:10.1038/6136