Domain characteristics of the carboxyl-terminal fragment 206-316 of thermolysin: unfolding thermodynamics
- 12 October 1982
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 21 (21) , 5196-5202
- https://doi.org/10.1021/bi00264a014
Abstract
No abstract availableThis publication has 21 references indexed in Scilit:
- Thermodynamics of protein cross-linksBiochemistry, 1978
- Stability of phage T4 lysozymes I. Native properties and thermal stability of wild type and two mutant lysozymesBiochimica et Biophysica Acta (BBA) - Protein Structure, 1977
- Isolation and characterization of independently folding regions of the β chain of Escherichia coli tryptophan synthetaseBiochemistry, 1977
- 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
- Conformational and thermodynamic properties of apo A-1 of human plasma high density lipoproteins.Journal of Biological Chemistry, 1976
- Thermodynamic investigations of proteinsBiophysical Chemistry, 1976
- Thermodynamic investigations of proteinsBiophysical Chemistry, 1976
- Thermodynamic investigations of proteinsBiophysical Chemistry, 1976
- Evidence for Residual Structure in Acid- and Heat-denatured ProteinsJournal of Biological Chemistry, 1967
- Validity of the “two‐state” hypothesis for conformational transitions of proteinsBiopolymers, 1966