Sandbox Reserved 820: Difference between revisions

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m Add some scene about 2vaf structure.
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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.--!>
<!--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.-->


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>.
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>.
<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>.
<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 08:12, 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.
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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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There are 12 alpha helix and 15 beta sheet. The acidics amino acids can bind the Ca2+ especially the glutamate and the aspartate.

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