Sandbox Reserved 996: Difference between revisions
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Biologically, Ectatomin exists as a heterodimer stabilized by <scene name='69/691538/Cysteine_disulfide/1'>disulfide linkages</scene>. The <scene name='69/691538/Alpha_subunit/1'>α subunit</scene> has 37 amino acid residues, while the <scene name='69/691538/Beta_subunit/1'>β subunit</scene> has 34 amino acid residues. The structure of Ectatomin was solved using 2D NMR and CHARMm computational optimization, though there are 20 similar proposed models in total.<ref name="refone">PMID: 7881269</ref> | Biologically, Ectatomin exists as a heterodimer stabilized by <scene name='69/691538/Cysteine_disulfide/1'>disulfide linkages</scene>. The <scene name='69/691538/Alpha_subunit/1'>α subunit</scene> has 37 amino acid residues, while the <scene name='69/691538/Beta_subunit/1'>β subunit</scene> has 34 amino acid residues. The structure of Ectatomin was solved using 2D NMR and CHARMm computational optimization, though there are 20 similar proposed models in total.<ref name="refone">PMID: 7881269</ref> | ||
Generally, each subunit is composed of two antiparallel α-helices, linked by disulfide bonds, with a connecting hairpin hinge region. The two subunits are linked by a | Generally, each subunit is composed of two antiparallel α-helices, linked by disulfide bonds, with a connecting hairpin hinge region. The two subunits are linked by a disulfide bond between their hairpin hinge regions. One α-helix from each subunit is kinked approximately 40°, due to the presence of <scene name='69/691538/Prolines_both_subunits/2'>proline residues</scene>. The kinked α-helix of the α subunit is more kinked, containing three proline residues, while the kinked α-helix of the β subunit only contains one proline residue.<ref name="refone" /> | ||
The internal region between the two subunits is primarily composed of hydrophobic residues. | The internal region between the two subunits is primarily composed of hydrophobic residues. | ||
