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

Nature volume 330, pages 41–46 (1987)Cite this article

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.

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Author notes

  1. Tom Alber

    Present address: Department of Biochemistry, University of Utah School of Medicine, 50 N Medical Drive, Salt Lake City, Utah, 84132, USA

  2. Sean P. Cook

    Present address: Department of Biochemistry, University of Washington, Seattle, Washington, 98195, USA

Authors and Affiliations

  1. Institute of Molecular Biology and Department of Physics, University of Oregon, Eugene, Oregon, 97403, USA

    Tom Alber, Sun Dao-pin, Keith Wilson, Joan A. Wozniak, Sean P. Cook & Brian W. Matthews

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Alber, T., Dao-pin, S., Wilson, K. et al. Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. Nature 330, 41–46 (1987). https://doi.org/10.1038/330041a0

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