Sandbox Reserved 1109

This Sandbox is Reserved from 25/11/2019, through 30/9/2020 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1091 through Sandbox Reserved 1115.

To get started: Click the edit this page tab at the top. Save the page after each step, then edit it again. show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page. Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc. More help: Help:Editing

Your Heading Here (maybe something like 'Structure')

spinqualitylabelsall models 6flt, resolution 3.42Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia or to the article describing Jmol to the rescue. Structure The alpha-synuclein (1-121) (default scene) is about 14 kDa fibril constituted by two protofilaments of 121 residues . The presence of many ꞵ-sheet induce a Greek-key motif of 99Å diameter . Indeed, There are 8 Beta-strands interrupted by glycines TextToBeDisplayed, between the residues 42 to about 102 . 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. Disease One of the main characteristics of Neurodegenerative disorders is the loss of the protective capacity surrounding the neurons or the gain of the toxic proteins. The mechanism by which the neuronal damage occurs is due to specific mutations, or other alterations of the synaptic proteins. Recently, two main hypotheses have been developed surrounding Parkinson's disease research. Firstly, the missense mutation of the α-synuclein gene is a rare genetic disorder that cause Parkinson's disease. Secondly, the α-synuclein protein is the main component of Lewy bodies and Lewy neurites which are defining pathological characteristics of all Parkinson's disease cases. Structural highlights This is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.