Evidence for intermediates during unfolding and refolding of a two-domain protein: phage T4 lysozyme equilibrium and kinetic studies
- 3 January 1984
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 23 (1) , 11-19
- https://doi.org/10.1021/bi00296a003
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 4 references indexed in Scilit:
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- Preparation and characterization of a modified form of beta2 subunit of Escherichia coli tryptophan synthetase suitable for investigating protein folding.Proceedings of the National Academy of Sciences, 1977
- Antibody as an immunological probe for studying the refolding of bovine serum albumin. I. The catalysis of reoxidation of reduced bovine serum albumin by glutathione and a disulfide interchange enzyme.Journal of Biological Chemistry, 1976
- Structural patterns in globular proteinsNature, 1976