Sandbox 42: Difference between revisions
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The primary catalytic action of the enzyme lysozyme is to hydrolyze β(1→4) glycosidic linkages found in bacterial cell walls.<ref>http://lysozyme.co.uk/</ref> More specifically, lysozyme hydrolyzes the linkages from ''N''-acetylmuramic acid to ''N''-acetylglucosamine which occur in peptidoglycans of the cell wall. The small 14.3 kD Hen egg white lysozyme is one of the most widely studied lysozymes. | The primary catalytic action of the enzyme lysozyme is to hydrolyze β(1→4) glycosidic linkages found in bacterial cell walls.<ref>http://lysozyme.co.uk/</ref> More specifically, lysozyme hydrolyzes the linkages from ''N''-acetylmuramic acid to ''N''-acetylglucosamine which occur in peptidoglycans of the cell wall. The small 14.3 kD Hen egg white lysozyme is one of the most widely studied lysozymes. | ||
== Secondary structure == | == Secondary structure == | ||
Hen egg white lysozyme is formed from one polypetide chain 129 amino acids in length. Important <scene name='Sandbox_42/Secondary_structures/2'> | Hen egg white lysozyme is formed from one polypetide chain 129 amino acids in length. Important <scene name='Sandbox_42/Secondary_structures/2'>seconday structures</scene> formed by the chain include 7 alpha helicies and 1 beta sheet consisting of 3 anti-parallel strands. 4 disulfide bonds are involved in folding of the chain. | ||
== Distribution of residue polarity == | == Distribution of residue polarity == | ||
The <scene name='Sandbox_42/Hydrophobic-polar/1'>distribution of hydrophobic and polar residues</scene> in lysozyme is varied, with both types of residues on the surface of the enzyme. | The <scene name='Sandbox_42/Hydrophobic-polar/1'>distribution of hydrophobic and polar residues</scene> in lysozyme is varied, with both types of residues on the surface of the enzyme. | ||
