Sandbox Reserved 1661: Difference between revisions
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Somatotropin has three major isoforms. The predominant form is composed out of 191 amino acids and has a molecular weight of 22 kDa. | Somatotropin has three major isoforms. The predominant form is composed out of 191 amino acids and has a molecular weight of 22 kDa. | ||
The '''primary structure''', corresponding to a sequence of amino acids, of the predominant somatotropin is the following : | The '''primary structure''', corresponding to a sequence of amino acids, of the predominant somatotropin is the following : | ||
PUT IMAGE | |||
Somatotropin does not exist as a linear chain of amino acids, it twists and folds on itself, forming the '''secondary structure'''. The protein, made up of a single chain, consists of four antiparallel aligned <scene name='86/868194/Halpha/1'>α-helices</scene> in an up-up-down-down manner <ref name="Endokrynologika Polska">DOI:10.5603/EP.2013.0009</ref> [https://doi.org/10.1016/j.ghir.2013.02.002]. 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. All helices are ampipathic with strong hydrophobic regions, especially helix 2 is very hydrophobic. The hydrophobic protein core is usually tigthly packed and any mutations in the hidden positions lead to destablilization <ref name="pubMed">PMID:17584122</ref>. | Somatotropin does not exist as a linear chain of amino acids, it twists and folds on itself, forming the '''secondary structure'''. The protein, made up of a single chain, consists of four antiparallel aligned <scene name='86/868194/Halpha/1'>α-helices</scene> in an up-up-down-down manner <ref name="Endokrynologika Polska">DOI:10.5603/EP.2013.0009</ref> [https://doi.org/10.1016/j.ghir.2013.02.002]. 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. All helices are ampipathic with strong hydrophobic regions, especially helix 2 is very hydrophobic. The hydrophobic protein core is usually tigthly packed and any mutations in the hidden positions lead to destablilization <ref name="pubMed">PMID:17584122</ref>. | ||
