1L17: HYDROPHOBIC STABILIZATION IN T4 LYSOZYME DETERMINED DIRECTLY BY MULTIPLE SUBSTITUTIONS OF ILE 3

Citation:
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.
PDB ID: 1L17Download
MMDB ID: 56610
PDB Deposition Date: 1989/5/1
Updated in MMDB: 2017/12
Experimental Method:
x-ray diffraction
Resolution: 1.7  Å
Source Organism:
Similar Structures:
Biological Unit for 1L17: monomeric; determined by author
Molecular Components in 1L17
Label Count Molecule
Protein (1 molecule)
1
T4 Lysozyme(Gene symbol: e)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
.