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Title
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Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3.
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Authors
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M.Matsumura,
W.J.Becktel,
B.W.Matthews.
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Ref.
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Nature, 1988,
334,
406-410.
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PubMed id
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Abstract
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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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