Article
Perturbation of Trp 138 in T4 lysozyme by mutations at Gln 105 used to correlate changes in structure, stability, solvation, and spectroscopic properties.
Proteins - 1 Apr 1993
Pjura P, McIntosh L P, Wozniak J A, Matthews B W
Abstract excerpt
In order to correlate between spectroscopic and structural changes in a protein, the environment of Trp 135 in T4 lysozyme was deliberately perturbed by the replacement of Gln 105 with alanine (Q105A), glycine (Q105G), and glutamic acid (Q105E). In wild-type lysozyme, Trp 135 is buried, but the indole nitrogen is hydrogen-bonded to the side-chain of Gln 105. In the Q105G and Q105A mutant structures, the indole...
Topics
- Bacteriophage T4
- Crystallography
- Fluorescence Polarization
- Glutamine
- Magnetic Resonance Spectroscopy
- Mercaptoethanol
- Models, Molecular
- Muramidase
- Mutation
- Protein Conformation
- Solubility