Sandbox 39
From Proteopedia
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LYSOZYME
Lysozyme is a powerful enzyme of biological significance found in abundance in tears, saliva, and human milk. It is also known as muramidase, or glycocide hydrolase. It is known for damaging bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. In this way, lysozyme is efficient in lysing the cell walls of both bacteria and fungi.
A simple cartoon structure of lysozyme can be seen to the right. The secondary structures can be seen in blue, and the salt bridges are highlighted in yellow. The following sections will highlight different subsections of the lysozyme protein using colors and labels through the program Jmol.
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Secondary Structure
The structure of lysozyme with its secondary structures highlighted in yellow and pink can be seen to your left by clicking on: . The structures highlight the alpha helicies, and the yellow lines highlight the beta-pleated sheets. Lysozyme contains five alpha helicies and five beta-pleated sheets. Three of the beta-pleated sheets are antiparallel to one another, and the other two are separate from each other.
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Hydrophobicity
Lysozyme contain both hydrophobic, or water-hating, regions and hydrophillic, or water-loving, regions. These regions can be displayed with the hydrophobic regions in gray and the polar, hydrophillic regions in purple by clicking on the following link: .
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