Sandbox 42: Difference between revisions
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Hen egg white lysozyme is formed from one polypetide chain 129 amino acids in length. Important <scene name='Sandbox_42/Secondary_structures/2'>secondary 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. | Hen egg white lysozyme is formed from one polypetide chain 129 amino acids in length. Important <scene name='Sandbox_42/Secondary_structures/2'>secondary 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. | |||
== Active site and Binding == | == Active site and Binding == | ||
