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Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3

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Abstract

Replacing the isoleucine at amino-acid position three of bacteriophage T4 lysozyme causes changes in the thermodynamic stability of the protein that are directly related to the hydrophobicity of the substituted residue. Structural analysis confirms that the hydrophobic stabilization is proportional to the reduction of the surface area accessible to solvent on folding.

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Authors and Affiliations

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

    Masazumi Matsumura, Wayne J. Becktel & Brian W. Matthews

Authors
  1. Masazumi Matsumura
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  2. Wayne J. Becktel
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  3. Brian W. Matthews
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Matsumura, M., Becktel, W. & Matthews, B. Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. Nature 334, 406–410 (1988). https://doi.org/10.1038/334406a0

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