Structural studies of mutants of T4 lysozyme that alter hydrophobic stabilization.

  title={Structural studies of mutants of T4 lysozyme that alter hydrophobic stabilization.},
  author={Masazumi Matsumura and Joan A. Wozniak and Dingyou Sun and Brian W. Matthews},
  journal={The Journal of biological chemistry},
  volume={264 27},
Multiple replacements at amino acid position 3 of bacteriophage T4 lysozyme have shown that the conformational stability of the protein is directly governed by the hydrophobicity of the residue substituted (Matsumura, M., Becktel, W. J., and Matthews, B. W. (1988) Nature 334, 406-410). Of the 13 mutant lysozymes made by site-directed mutagenesis, two variants, one with valine (I3V) and the other with tyrosine (I3Y), were crystallized and their structures solved. In this report we describe the… CONTINUE READING


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