Sandbox Reserved 1109: Difference between revisions
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== Structure == | == Structure == | ||
The alpha-synuclein (1-121) (default 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 99Å diameter <ref>DOI 10.1038/s41467-018-05971-2</ref>. Indeed, There are 8 | The alpha-synuclein (1-121) (default 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 99Å diameter <ref>DOI 10.1038/s41467-018-05971-2</ref>. Indeed, There are 8 <scene name='82/829362/Beta-strands/1'>Beta-strands</scene> interrupted by glycines, between the residues 42 to about 102 <ref>DOI 10.7554/eLife.36402</ref>. | ||
Two structures coincide thanks to the presence of hydrophobic and hydrophilic regions. A hydrophobic intra-molecular core between the two protofilaments is formed by alanines, valines and one isoleucine. A hydrophilic channel contains majority of threonines. To stabilize the protein in an aqueous solution, there are solvent exposed charged residues : Lysine and glutamic acid. | Two structures coincide thanks to the presence of hydrophobic and hydrophilic regions. A hydrophobic intra-molecular core between the two protofilaments is formed by alanines, valines and one isoleucine. A hydrophilic channel contains majority of threonines. To stabilize the protein in an aqueous solution, there are solvent exposed charged residues : Lysine and glutamic acid. | ||
