title: Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3.
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.
authors.affiliation: Institute of Molecular Biology, University of Oregon, Eugene 97403.
authors.forename: M
authors.initials: M
authors.lastname: Matsumura
authors.forename: W J
authors.initials: WJ
authors.lastname: Becktel
authors.forename: B W
authors.initials: BW
authors.lastname: Matthews
mesh_terms: D000596:Amino Acids / Q000032:analysis; D006358:Hot Temperature; D007532:Isoleucine; D008958:Models, Molecular; D009113:Muramidase / Q000032:analysis / Q000378:metabolism*; D013329:Structure-Activity Relationship; D013604:T-Phages / Q000201:enzymology*; D013816:Thermodynamics; D014961:X-Ray Diffraction
chemical_list: D000596:Amino Acids; D007532:Isoleucine; D009113:Muramidase