Folding and oxidation of recombinant human granulocyte colony stimulating factor produced in Escherichia coli. Characterization of the disulfide-reduced intermediates and cysteine—-serine analogs.-Reference-Cited by-同舟云学术

Folding and oxidation of recombinant human granulocyte colony stimulating factor produced in Escherichia coli. Characterization of the disulfide-reduced intermediates and cysteine—-serine analogs.

Published:1992-05 Issue:13 Volume:267 Page:8770-8777
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Lu H.S.,Clogston C.L.,Narhi L.O.,Merewether L.A.,Pearl W.R.,Boone T.C.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference28 articles.

1. Protein Folding;Fhelis,1982

2. Specific Intermediates in the Folding Reactions of Small Proteins and the Mechanism of Protein Folding

3. [5]Disulfide bonds as probes of protein folding pathways

4. Conformational restrictions on the pathway of folding and unfolding of the pancreatic trypsin inhibitor

5. Energetics of folding and unfolding of pancreatic trypsin inhibitor

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