Thermal denaturation of bacteriophage T4 lysozyme at neutral pH
Open Access
- 1 May 1987
- journal article
- research article
- Published by Wiley in Peptide Science
- Vol. 26 (5), 619-623
- https://doi.org/10.1002/bip.360260505
Abstract
No abstract availableThis publication has 10 references indexed in Scilit:
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- Thermodynamic stability and point mutations of bacteriophage T4 lysozymeJournal of Molecular Biology, 1984
- Amino acid substitutions far from the active site of bacteriophage T4 lysozyme reduce catalytic activity and suggest that the C-terminal Lobe of the enzyme participates in substrate bindingJournal of Molecular Biology, 1982
- Mutations and protein stabilityPeptide Science, 1981
- Molecular basis of thermostability in the lysozyme from bacteriophage T4Nature, 1979
- Structure of the lysozyme from bacteriophage T4: An electron density map at 2.4 Å resolutionJournal of Molecular Biology, 1978
- Phage T4 lysozyme Physical properties and reversible unfoldingBiochimica et Biophysica Acta (BBA) - Protein Structure, 1975