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 in an up-up-down-down manner <ref name="Endokrynologika Polska">DOI:10.5603/EP.2013.0009</ref>. 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 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>. 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>. | ||
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 stabilised 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 stabilised 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. | ||
