Structure-based statistical thermodynamic analysis of T4 lysozyme mutants: structural mapping of cooperative interactions
Open Access
- 28 February 1997
- journal article
- Published by Elsevier in Biophysical Chemistry
- Vol. 64 (1-3), 69-79
- https://doi.org/10.1016/s0301-4622(96)02220-x
Abstract
No abstract availableKeywords
This publication has 50 references indexed in Scilit:
- Temperature and pH Dependences of Hydrogen Exchange and Global Stability for Ovomucoid Third DomainBiochemistry, 1996
- Different Subdomains are Most Protected From Hydrogen Exchange in the Molten Globule and Native States of Human α-LactalbuminJournal of Molecular Biology, 1995
- Elucidating the Folding Problem of Helical Peptides using Empirical Parameters. II†. Helix Macrodipole Effects and Rational Modification of the Helical Content of Natural PeptidesJournal of Molecular Biology, 1995
- Determination of α-Helix Propensity within the Context of a Folded ProteinJournal of Molecular Biology, 1994
- Temperature and guanidine hydrochloride dependence of the structural stability of ribonuclease T1Biochemistry, 1992
- α-Helix stability in proteinsJournal of Molecular Biology, 1992
- Molecular basis of co-operativity in protein foldingJournal of Molecular Biology, 1991
- A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozymeBiochemistry, 1991
- Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozymeNature, 1987
- The interpretation of protein structures: Estimation of static accessibilityJournal of Molecular Biology, 1971