Amyloid beta: Difference between revisions
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'''Amyloids''' are insoluble fibrous proteins | '''Amyloids''' are insoluble fibrous proteins | ||
The most reasonable structure determined structure consists of <scene name='Amyloid_beta/Two_helices/1'>two helices</scene>; the first helix (residues 8-25) is well defined and has an RMSD of 0.38 angstroms and the second (residues 28-38) is interrupted at the Ile32-Gly33 connection. The two helices are connected by a <scene name='Amyloid_beta/Kink/1'>kink</scene> (residues 26 and 27). | The most reasonable structure determined structure consists of <scene name='Amyloid_beta/Two_helices/1'>two helices</scene>; the first helix (residues 8-25) is well defined and has an RMSD of 0.38 angstroms and the second (residues 28-38) is interrupted at the Ile32-Gly33 connection. The two helices are connected by a <scene name='Amyloid_beta/Kink/1'>kink</scene> (residues 26 and 27). <ref>PMID: 12423364</ref> | ||
==References== | |||
<references/> | |||
Revision as of 00:49, 26 November 2011
<StructureSection load=1iyt size='500' side='right' caption='amyloid-beta(1-42)', (1dm0)' scene=>
IntroductionIntroduction
Alzheimer's disease is characterized by extracellular proteic plaques and intracellular neurofibrillary tangles. Amyloids are insoluble fibrous proteins
The most reasonable structure determined structure consists of ; the first helix (residues 8-25) is well defined and has an RMSD of 0.38 angstroms and the second (residues 28-38) is interrupted at the Ile32-Gly33 connection. The two helices are connected by a (residues 26 and 27). [1]