Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme

T Alber; D P Sun; K Wilson; J A Wozniak; S P Cook; B W Matthews

doi:10.1038/330041a0

Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme

Nature. 1987 Nov;330(6143):41-6. doi: 10.1038/330041a0.

Authors

T Alber¹, D P Sun, K Wilson, J A Wozniak, S P Cook, B W Matthews

Affiliation

¹ Department of Physics, University of Oregon, Eugene 97403.

PMID: 3118211
DOI: 10.1038/330041a0

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.

MeSH terms

Computer Simulation
Enzyme Stability
Escherichia coli / enzymology*
Hydrogen Bonding
Models, Molecular
Muramidase* / genetics
Mutation
Protein Conformation
T-Phages / enzymology*
Thermodynamics
Threonine*
X-Ray Diffraction

Substances

Threonine
Muramidase