Sandbox Reserved 1756: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 42: | Line 42: | ||
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. | |||
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> | ||
<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/Space_fill/1'>Space fill</scene> represent of how much of molecules have occupied at the active site. | ||
