A Pro to His mutation in active site of thioredoxin increases its disulfide-isomerase activity 10-fold. New refolding systems for reduced or randomly oxidized ribonuclease.-Reference-Cited by-同舟云学术

A Pro to His mutation in active site of thioredoxin increases its disulfide-isomerase activity 10-fold. New refolding systems for reduced or randomly oxidized ribonuclease.

Published:1992-05 Issue:13 Volume:267 Page:9047-9052
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Lundström J,Krause G,Holmgren A

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference37 articles.

1. THE KINETICS OF FORMATION OF NATIVE RIBONUCLEASE DURING OXIDATION OF THE REDUCED POLYPEPTIDE CHAIN

2. Experimental and Theoretical Aspects of Protein Folding

3. Identification of a protein required for disulfide bond formation in vivo

4. On the relevance of non-random polypeptide conformations for protein folding

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