Thermodynamic stability and point mutations of bacteriophage T4 lysozyme
- 1 May 1984
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 175 (2), 195-212
- https://doi.org/10.1016/0022-2836(84)90474-1
Abstract
No abstract availableThis publication has 26 references indexed in Scilit:
- 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
- Stability of phage T4 lysozomesBiochimica et Biophysica Acta (BBA) - Protein Structure, 1979
- Surface and inside volumes in globular proteinsNature, 1979
- Molecular basis of thermostability in the lysozyme from bacteriophage T4Nature, 1979
- 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
- The nature of the accessible and buried surfaces in proteinsJournal of Molecular Biology, 1976
- Vibrational states of the biopolymer polyglycine II: theory and experimentScience, 1975
- Phage T4 lysozyme Physical properties and reversible unfoldingBiochimica et Biophysica Acta (BBA) - Protein Structure, 1975
- Low‐frequency vibrational spectra of some homopolypeptides in the solid stateBiopolymers, 1973
- Structural Studies of Ribonuclease. V. Reversible Change of Configuration1-3Journal of the American Chemical Society, 1961