Sandbox Reserved 820

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m (Add some scene about 2vaf structure.)
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<scene name='56/568018/General_structure/3'>TextToBeDisplayed</scene>
<scene name='56/568018/General_structure/3'>TextToBeDisplayed</scene>
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<!--J'ai fais un peu joujou avec les animations pour montrer les hélices et les feuillets béta! Aussi tous les AA acides et plus particulièrement asp et glu.--!>
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There are <scene name='56/568018/Alpha_helix/1'>12 alpha helix</scene> and <scene name='56/568018/Beta_sheet/2'>15 beta sheet</scene>.
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<scene name='56/568018/Acidic_amino_acids/1'>The acidics amino acids</scene> can bind the Ca2+ especially the <scene name='56/568018/Glu/1'>glutamate</scene> and the <scene name='56/568018/Asp/1'>aspartate</scene>.

Revision as of 08:11, 29 December 2013

This Sandbox is Reserved from 06/12/2018, through 30/06/2019 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1480 through Sandbox Reserved 1543.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • Click the 3D button (when editing, above the wikitext box) to insert Jmol.
  • 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

Introduction

Calsequestrin-2 (or CASQ2) is the soluble CA2+ binding protein in the sarcoplasmic reticulum lumen of the cardiac muscle cells. CASQ2 could be either in a monomeric, homodimeric, or homooligomeric chain form depending on its bounds with Ca2+. Mutations of CASQ2 are involved in cardiac diseases such as Catecholaminergic Polymorphic Ventricular Tachycardia.



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