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PMID: 3118211 Published · ppublish English Journal Article 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.

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

Nature ·Vol. 330 ·No. 6143 ·1987-00-00 ·Pages 41-6

Alber T, Sun DP, Wilson K, Wozniak JA, Cook SP, Matthews BW

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.

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

Chemicals

Threonine Muramidase

Authors & Affiliations

6 authors, click to expand affiliations / ORCID

Alber T

Department of Physics, University of Oregon, Eugene 97403.

Sun D P

Wilson K

Wozniak J A

Cook S P

Matthews B W

Article Info

Journal

Nature

Abbr.

Nature

ISSN

0028-0836

DOI

10.1038/330041a0

Published

1987-00-00

Pages

41-6

Language

English

Region

England

NLM ID

0410462

Subset

External Links

PubMed source DOI: 10.1038/330041a0 View journal details

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

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