Sandbox Reserved 1109: Difference between revisions

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== Structure ==

The <scene name='82/829362/Default_scene/4'>alpha-synuclein (1-121)</scene> is about 14 kDa fibril constituted by two protofilaments of 121 residues <ref>DOI 10.7554/eLife.36402</ref>. The presence of many ꞵ-sheet induce a Greek-key motif of 99 Å diameter <ref>DOI 10.1038/s41467-018-05971-2</ref>. Indeed, There are 8 <scene name='82/829362/beta-strands/6'>beta-strands interrupted by glycines</scene>, between the residues 42 to about 102 forming the ꞵ-arch <ref>DOI 10.7554/eLife.36402</ref>. These glycines help the folding of the molecule by their small size. The ꞵ-arch is stabilized by <scene name='82/829362/Hydrogen_bond/1'>hydrogen bonds N65-G68 and Q79-G86</scene>.

The <scene name='82/829362/Default_scene/4'>alpha-synuclein (1-121)</scene> is about 14 kDa fibril constituted by two protofilaments of 121 residues <ref>DOI 10.7554/eLife.36402</ref>. The presence of many ꞵ-sheet induce a Greek-key motif of 99 Å diameter <ref>DOI 10.1038/s41467-018-05971-2</ref>. Indeed, There are 8 <scene name='82/829362/beta-strands/7'>beta-strands interrupted by glycines</scene>, between the residues 42 to about 102 forming the ꞵ-arch <ref>DOI 10.7554/eLife.36402</ref>. These glycines help the folding of the molecule by their small size. The ꞵ-arch is stabilized by <scene name='82/829362/Hydrogen_bond/1'>hydrogen bonds N65-G68 and Q79-G86</scene>.

Two structures coincide thanks to the presence of <scene name='82/829362/Hydrophobic/3'>hydrophobic (red) and hydrophilic(blue) regions</scene>. A hydrophobic intra-molecular core between the two protofilaments is formed by <scene name='82/829362/Hydrophobic_ala_val_ile/3'>alanines, valines and one isoleucine</scene><ref>DOI 10.7554/eLife.36402</ref>. Residues from 54 to 75 form a <scene name='82/829362/Hydrophilic_channel/5'>hydrophilic channel</scene> which contains majority of threonines and glutamic acid<ref>DOI 10.7554/eLife.36402</ref>. To stabilize the protein in an aqueous solution, there are solvent-exposed charged residues: <scene name='82/829362/Hydrophobic_glu_lys/2'>Lysine and glutamic acid</scene>.

Sandbox Reserved 1109: Difference between revisions

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@@ Line 12: / Line 12: @@
 == Structure ==
-The <scene name='82/829362/Default_scene/4'>alpha-synuclein (1-121)</scene> is about 14 kDa fibril constituted by two protofilaments of 121 residues <ref>DOI 10.7554/eLife.36402</ref>. The presence of many ꞵ-sheet induce a Greek-key motif of 99 Å diameter <ref>DOI 10.1038/s41467-018-05971-2</ref>. Indeed, There are 8 <scene name='82/829362/beta-strands/6'>beta-strands interrupted by glycines</scene>, between the residues 42 to about 102 forming the ꞵ-arch <ref>DOI 10.7554/eLife.36402</ref>. These glycines help the folding of the molecule by their small size. The ꞵ-arch is stabilized by <scene name='82/829362/Hydrogen_bond/1'>hydrogen bonds N65-G68 and Q79-G86</scene>.
+The <scene name='82/829362/Default_scene/4'>alpha-synuclein (1-121)</scene> is about 14 kDa fibril constituted by two protofilaments of 121 residues <ref>DOI 10.7554/eLife.36402</ref>. The presence of many ꞵ-sheet induce a Greek-key motif of 99 Å diameter <ref>DOI 10.1038/s41467-018-05971-2</ref>. Indeed, There are 8 <scene name='82/829362/beta-strands/7'>beta-strands interrupted by glycines</scene>, between the residues 42 to about 102 forming the ꞵ-arch <ref>DOI 10.7554/eLife.36402</ref>. These glycines help the folding of the molecule by their small size. The ꞵ-arch is stabilized by <scene name='82/829362/Hydrogen_bond/1'>hydrogen bonds N65-G68 and Q79-G86</scene>.
 Two structures coincide thanks to the presence of <scene name='82/829362/Hydrophobic/3'>hydrophobic (red) and hydrophilic(blue) regions</scene>. A hydrophobic intra-molecular core between the two protofilaments is formed by <scene name='82/829362/Hydrophobic_ala_val_ile/3'>alanines, valines and one isoleucine</scene><ref>DOI 10.7554/eLife.36402</ref>. Residues from 54 to 75  form a <scene name='82/829362/Hydrophilic_channel/5'>hydrophilic channel</scene> which contains majority of threonines and glutamic acid<ref>DOI 10.7554/eLife.36402</ref>. To stabilize the protein in an aqueous solution, there are solvent-exposed charged residues: <scene name='82/829362/Hydrophobic_glu_lys/2'>Lysine and glutamic acid</scene>.