Thermodynamic stability and point mutations of bacteriophage T4 lysozyme.


The thermodynamics of melting of bacteriophage T4 lysozyme and four of its mutants have been measured by van't Hoff methods. The effect of pH has been explored and utilized to obtain the dependence of the enthalpy on temperature as suggested by Privalov and co-workers. The enthalpy change is a steep linear function of temperature. delta Cp is large and constant within experimental error. Changes in delta Hu are as large as 30% for a single point mutation. Changes in enthalpy are largely compensated by changes in entropy. Changes in stability, as measured by the free energy of unfolding, are smaller than those of delta H, but are very large in a relative sense, since delta G is very much smaller than delta H. Origins of the destabilization caused by mutations are discussed. Study holds ProTherm entries: 1210, 1211, 1212, 1213, 1214, 11782, 11783, 11784, 13610, 13611 Extra Details: dG was measured at 47 degrees C bacteriophage T4 lysozyme; free energies of unfolding;,point mutation; thermodynamic stability

Submission Details

ID: Erm2ShUW3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:16 p.m.

Version: 1

Publication Details
Hawkes R;Grutter MG;Schellman J,J. Mol. Biol. (1984) Thermodynamic stability and point mutations of bacteriophage T4 lysozyme. PMID:6726809
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Endolysin P00720 ENLYS_BPT4