1l18
| |||||||
| , resolution 1.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HYDROPHOBIC STABILIZATION IN T4 LYSOZYME DETERMINED DIRECTLY BY MULTIPLE SUBSTITUTIONS OF ILE 3
OverviewOverview
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.
About this StructureAbout this Structure
1L18 is a Single protein structure of sequence from Bacteriophage t4. Full crystallographic information is available from OCA.
ReferenceReference
Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3., Matsumura M, Becktel WJ, Matthews BW, Nature. 1988 Aug 4;334(6181):406-10. PMID:3405287
Page seeded by OCA on Thu Mar 20 12:24:58 2008