Sandbox Reserved 1806: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Ivan Munoz (talk | contribs) No edit summary |
Ivan Munoz (talk | contribs) No edit summary |
||
| Line 25: | Line 25: | ||
== Structural highlights == | == Structural highlights == | ||
The secondary structure of a protein contains regions of amino acid chains that are stabilized by hydrogen bonds which create alpha-helix and beta-pleated sheets. For Pyrrolysine tRNA synthetase, the secondary structure has 2 domains, one called the N-terminal and the other being the C-terminal. Pyrrolysine is a modified lysine with a 4-methylpyrroline-5-carboxylate group linked by an amide to the ɛ-amino group. Pyrrolysine is lysine in which has a pyrroline ring linked to the end of the lysine side chain. | The secondary structure of a protein contains regions of amino acid chains that are stabilized by hydrogen bonds which create alpha-helix and beta-pleated sheets. For Pyrrolysine tRNA synthetase, the <scene name='95/954103/Secondary_structure/1'>secondary structure</scene> has 2 domains, one called the N-terminal and the other being the C-terminal. Pyrrolysine is a modified lysine with a 4-methylpyrroline-5-carboxylate group linked by an amide to the ɛ-amino group. Pyrrolysine is lysine in which has a pyrroline ring linked to the end of the lysine side chain. | ||
The ''tertiary structure'' of a protein is the overall 3D structure of the protein. The protein is stabilized by outside polar hydrophilic hydrogen and ionic bond interactions, and internal hydrophobic interactions between non-polar amino acid side chains. | The ''tertiary structure'' of a protein is the overall 3D structure of the protein. The protein is stabilized by outside polar hydrophilic hydrogen and ionic bond interactions, and internal hydrophobic interactions between non-polar amino acid side chains. | ||
