Sandbox k11v: Difference between revisions

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==Toxic Amyloid Small Oligomer’s atomic view==

The interactive Molecular Tour below assumes that you are familiar with the journal article<ref>PMID:22403391</ref>.

== Introduction ==

Amyloid fibrils were first assumed to be the agents of Amyloid diseases,including Alzheimer’s,Parkinson’s and the prion conditions.But studies from many laboratories suggest that the reason for this disorder are lower molecular weight entities known as small amyloid oligomers,instead of the associated protein fibrils.Segment of amyloid forming protein <scene name='77/771966/3l1g_full_structure/1'>~~αβ~~ crystallin(ABC)</scene> makes oligomeric complex which exhibits properties of other amyloid oligomers.They are rich in beta-sheet structure and these oligomer can be identified by a conformational antibody(A11) that binds oligomers but not fibrils,irrespective of sequence of constituent protein.This protein is a chaperone that forms amyloid fibrils.The structure of oligomer shows a cylindrical barrel,made up of six anti-parallel protein strands known as cylindrin.This segment(coloured in black) termed as <scene name='77/771966/K11v_in_black/1'>K11V</scene> forms the cylindrin structure.

Amyloid fibrils were first assumed to be the agents of Amyloid diseases,including Alzheimer’s,Parkinson’s and the prion conditions.But studies from many laboratories suggest that the reason for this disorder are lower molecular weight entities known as small amyloid oligomers,instead of the associated protein fibrils.Segment of amyloid forming protein <scene name='77/771966/3l1g_full_structure/1'> crystallin(ABC)</scene> makes oligomeric complex which exhibits properties of other amyloid oligomers.They are rich in beta-sheet structure and these oligomer can be identified by a conformational antibody(A11) that binds oligomers but not fibrils,irrespective of sequence of constituent protein.This protein is a chaperone that forms amyloid fibrils.The structure of oligomer shows a cylindrical barrel,made up of six anti-parallel protein strands known as cylindrin.This segment(coloured in black) termed as <scene name='77/771966/K11v_in_black/1'>K11V</scene> forms the cylindrin structure.

== Molecular Tour ==

Sandbox k11v: Difference between revisions

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 ==Toxic Amyloid Small Oligomer’s atomic view==
-<StructureSection load='3l1g' size='300' side='centre' caption='Structure of &alpha;&beta; crystallin(ABC).PDB Id:3l1g' scene=''>
+<StructureSection load='3l1g' size='300' side='centre' caption='Structure of  crystallin(ABC).PDB Id:3l1g' scene=''>
 The interactive Molecular Tour below assumes that you are familiar with the journal article<ref>PMID:22403391</ref>.
 == Introduction ==
-Amyloid fibrils were first assumed to be the agents of Amyloid diseases,including Alzheimer’s,Parkinson’s and the prion conditions.But studies from many laboratories suggest that the reason for this disorder are lower molecular weight entities known as small amyloid oligomers,instead of the associated protein fibrils.Segment of amyloid forming protein <scene name='77/771966/3l1g_full_structure/1'>&alpha;&beta; crystallin(ABC)</scene> makes oligomeric complex which exhibits properties of other amyloid oligomers.They are rich in beta-sheet structure and these oligomer can be identified by a conformational antibody(A11) that binds oligomers but not fibrils,irrespective of sequence of constituent protein.This protein is a chaperone that forms amyloid fibrils.The structure of oligomer shows a cylindrical barrel,made up of six anti-parallel protein strands known as cylindrin.This segment(coloured in black) termed as <scene name='77/771966/K11v_in_black/1'>K11V</scene> forms the cylindrin structure.
+Amyloid fibrils were first assumed to be the agents of Amyloid diseases,including Alzheimer’s,Parkinson’s and the prion conditions.But studies from many laboratories suggest that the reason for this disorder are lower molecular weight entities known as small amyloid oligomers,instead of the associated protein fibrils.Segment of amyloid forming protein <scene name='77/771966/3l1g_full_structure/1'> crystallin(ABC)</scene> makes oligomeric complex which exhibits properties of other amyloid oligomers.They are rich in beta-sheet structure and these oligomer can be identified by a conformational antibody(A11) that binds oligomers but not fibrils,irrespective of sequence of constituent protein.This protein is a chaperone that forms amyloid fibrils.The structure of oligomer shows a cylindrical barrel,made up of six anti-parallel protein strands known as cylindrin.This segment(coloured in black) termed as <scene name='77/771966/K11v_in_black/1'>K11V</scene> forms the cylindrin structure.
 == Molecular Tour ==