Sandbox Reserved 1756: Difference between revisions
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Important <scene name='93/934000/Main_secondary_features/1'>main secondary features</scene> to stabilize the protein | Important <scene name='93/934000/Main_secondary_features/1'>main secondary features</scene> to stabilize the protein | ||
he pink helix represents the alpha helix, and the yellow sheet represents | |||
the beta sheet. Each C=O consists of two oxygen atoms that form | |||
hydrogen bonds, which stabilize the secondary structure. A polar amino | |||
acid residue is on the outside and a nonpolar amino acid is inside the alpha | |||
helix since non-polar amino acids do not react with water. Beta sheet runs | |||
in an antiparallel direction of non-polar and polar amino acids. | |||
<scene name='93/934000/Features_of_quaternary/1'> Homodimer is quaternary structure and HOAT cotains homodimer.</scene> | <scene name='93/934000/Features_of_quaternary/1'> Homodimer is quaternary structure and HOAT cotains homodimer.</scene> | ||
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<scene name='93/934000/Aa_aromatic/1'>Aromatic rings</scene> plays a role important role in protein structure and ligand binding. Aromatic ring is important of protein interaction that allows pi stacking and acts as acceptor for hydrogen bonds. It is important for protein structure and ligand binding. | <scene name='93/934000/Aa_aromatic/1'>Aromatic rings</scene> plays a role important role in protein structure and ligand binding. Aromatic ring is important of protein interaction that allows pi stacking and acts as acceptor for hydrogen bonds. It is important for protein structure and ligand binding. | ||
<scene name='93/934000/Aa_polar/1'> | <scene name='93/934000/Aa_polar/1'> | ||
