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

M Matsumura; W J Becktel; B W Matthews

doi:10.1038/334406a0

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

Nature. 1988 Aug 4;334(6181):406-10. doi: 10.1038/334406a0.

Authors

M Matsumura¹, W J Becktel, B W Matthews

Affiliation

¹ Institute of Molecular Biology, University of Oregon, Eugene 97403.

PMID: 3405287
DOI: 10.1038/334406a0

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.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.

MeSH terms

Amino Acids / analysis
Hot Temperature
Isoleucine*
Models, Molecular
Muramidase / analysis
Muramidase / metabolism*
Structure-Activity Relationship
T-Phages / enzymology*
Thermodynamics
X-Ray Diffraction

Substances

Amino Acids
Isoleucine
Muramidase