Sandbox Reserved 996: Difference between revisions

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== Structure ==

Biologically, Ectatomin exists as a heterodimer stabilized by <scene name='69/691538/Jsmol_stop_being_shit/1'>α subunit</scene> linkages. 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 ~~conformations~~.

Biologically, Ectatomin exists as a heterodimer stabilized by <scene name='69/691538/Jsmol_stop_being_shit/1'>α subunit</scene> linkages. 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.

Generally, each subunit is composed of two α-helices, linked by disulfide bonds, with a connecting hairpin hinge region. The two subunits are linked by a disfulide bond between their hairpin hinge regions. One α-helix from each subunit is kinked, due to the presence of proline residues. 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.

Generally, each subunit is composed of two α-helices, linked by disulfide bonds, with a connecting hairpin hinge region. The two subunits are linked by a disfulide bond between their hairpin hinge regions. One α-helix from each subunit is kinked, due to the presence of <scene name='69/691538/Prolines_both_subunits/1'>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.

Sandbox Reserved 996: Difference between revisions

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 == Structure ==
-Biologically, Ectatomin exists as a heterodimer stabilized by <scene name='69/691538/Jsmol_stop_being_shit/1'>α subunit</scene> linkages.  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 conformations.
+Biologically, Ectatomin exists as a heterodimer stabilized by <scene name='69/691538/Jsmol_stop_being_shit/1'>α subunit</scene> linkages.  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.
-Generally, each subunit is composed of two α-helices, linked by disulfide bonds, with a connecting hairpin hinge region.  The two subunits are linked by a disfulide bond between their hairpin hinge regions.  One α-helix from each subunit is kinked, due to the presence of proline residues.  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.
+Generally, each subunit is composed of two α-helices, linked by disulfide bonds, with a connecting hairpin hinge region.  The two subunits are linked by a disfulide bond between their hairpin hinge regions.  One α-helix from each subunit is kinked, due to the presence of <scene name='69/691538/Prolines_both_subunits/1'>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.