Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences.

Abstract excerpt

Two bulky amino acids within the core of phage T4 lysozyme have each been replaced in turn with a series of hydrophobic amino acids. In one set of experiments, Leu99 was replaced with Phe, Met, Ile, Val and Ala. In the second series, Phe153 was replaced with Leu, Met, Ile, Val and Ala. The double...

Topics

• Bacteriophage T4
• Enzyme Stability
• Leucine
• Models, Molecular
• Muramidase
• Mutation
• Phenylalanine
• Protein Conformation
• Thermodynamics
• Water
• X-Ray Diffraction