Molecular playground/beta 2 microglobulin

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<applet size='[450,338]' frame='true' align='right'
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<caption='β-2 Microglobulin' scene='User:Nick_Borotto/Sandbox_1/Basic_view/4' scene name='User:Nick_Borotto/Sandbox_1/Basic_view/4'>β-2 Microglobulin</scene> is a 12kd protein that self-assembles into amyloid fibrils in the presence of copper. This reaction is considered a likely cause for dialysis related amyloidosis; a disease where these fibrils build up in joints causing pain and eventually necessitating joint replacement.
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<caption='β-2 Microglobulin' scene='User:Nick_Borotto/Sandbox_1/Basic_view/4'>
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β-2 Microglobulin is a 12kd protein that self-assembles into amyloid fibrils in the presence of copper. This reaction is considered a likely cause for dialysis related amyloidosis; a disease where these fibrils build up in joints causing pain and eventually necessitating joint replacement.
Fibril assembly begins with the formation of a <scene name='User:Nick_Borotto/Sandbox_1/Proposed_dimer_structure/3'>Dimer</scene>. This structures formation is initiated when copper binds near the <scene name='User:Nick_Borotto/Sandbox_1/Metal_coordination_site/4'>N-terminus</scene>, this binding causes structural shifts throughout the protein, creating two new <scene name='User:Nick_Borotto/Sandbox_1/Proposed_dimer_interface/4'>planes</scene>. These planes interact in an antiparallel fashion forming the dimer.
Fibril assembly begins with the formation of a <scene name='User:Nick_Borotto/Sandbox_1/Proposed_dimer_structure/3'>Dimer</scene>. This structures formation is initiated when copper binds near the <scene name='User:Nick_Borotto/Sandbox_1/Metal_coordination_site/4'>N-terminus</scene>, this binding causes structural shifts throughout the protein, creating two new <scene name='User:Nick_Borotto/Sandbox_1/Proposed_dimer_interface/4'>planes</scene>. These planes interact in an antiparallel fashion forming the dimer.

Revision as of 16:00, 30 April 2010

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Tyler Marcinko, Nick Borotto, David Canner, Michal Harel

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