Sandbox Reserved 1661: Difference between revisions
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Somatotropin does not exist as a linear chain of amino acids, it twists and folds on itself, forming the '''secondary structure'''. The protein consists of four antiparallel aligned α-helices. The first helix starts at the 6th amino acid, which is a leucine and ends with the 37th amino acid proline. It is separated from the other three helices after the 37th position. The 38th and 39th amino acids, which are lysine and glutamic acid are spliced out of the protein and therefore disconnects the first helix from the second one. The second helix starts at position 72 till 92, the third from 106 till 128 and the fourth helix from 155 until 184. | Somatotropin does not exist as a linear chain of amino acids, it twists and folds on itself, forming the '''secondary structure'''. The protein consists of four antiparallel aligned α-helices. The first helix starts at the 6th amino acid, which is a leucine and ends with the 37th amino acid proline. It is separated from the other three helices after the 37th position. The 38th and 39th amino acids, which are lysine and glutamic acid are spliced out of the protein and therefore disconnects the first helix from the second one. The second helix starts at position 72 till 92, the third from 106 till 128 and the fourth helix from 155 until 184. | ||
From the secondary structure, we obtain the '''tertiary structure''', which corresponds to the 3D structure adopted by all the alpha helixes. The structural maintenance is ensured by electrostatic, hydrophobic, hydrogen and/or covalent interactions with cysteine 53 and cysteine 165 that form a disulphide bridge as well as cysteine 182 with cysteine 189. | From the secondary structure, we obtain the '''tertiary structure''', which corresponds to the 3D structure adopted by all the alpha helixes. The structural maintenance is ensured by electrostatic, hydrophobic, hydrogen and/or covalent interactions with cysteine 53 and cysteine 165 that form a disulphide bridge as well as cysteine 182 with cysteine 189. | ||
The protein has two different binding sites: both located at the ends of the protein, the N-terminus as well as the C-terminus. | The protein has two different binding sites: both located at the ends of the protein, the N-terminus as well as the C-terminus. | ||
It exists large number of reports published on structre-function relationship of GH using chemical modifications, proteolytic digestion or molecular biological methods to alter or delete amino acids or regions. | |||
== HGH receptors and interactions == | == HGH receptors and interactions == | ||
