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 | ||
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/Space_fill/1'>Space fill</scene> represent of how much of molecules have occupied at the active site | <scene name='93/934000/Features_of_quaternary/1'> Homodimer is quaternary structure and HOAT cotains homodimer.</scene> | ||
<scene name='93/934000/Space_fill/1'>Space fill</scene> represent of how much of molecules have occupied at the active site. | |||
== Other important features == | == Other important features == | ||
<scene name='93/934000/ | <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'> | |||
Polar amino acids</scene> is important part of protein structure. It is found usually on the outside of the alpha and beta that is because of its water-loving quality. It help to determine the 3-D structure and its specifically function. | |||
