Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme.
Measurements of changes in structure and stability caused by 13 different substitutions for threonine 157 in phage T4 lysozyme show that the most stable lysozyme variants contain hydrogen bonds analogous to those in the wild-type enzyme and that structural adjustments allow the protein to be surprisingly tolerant of amino-acid substitutions.
D003198:Computer Simulation; D004795:Enzyme Stability; D004926:Escherichia coli / Q000201:enzymology*; D006860:Hydrogen Bonding; D008958:Models, Molecular; D009113:Muramidase / Q000235:genetics; D009154:Mutation; D011487:Protein Conformation; D013604:T-Phages / Q000201:enzymology*; D013816:Thermodynamics; D013912:Threonine; D014961:X-Ray Diffraction
D013912:Threonine; D009113:Muramidase