Amyloid beta: Difference between revisions
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<StructureSection load=1iyt size='500' side='right' caption='amyloid-beta(1-42)', ([[1dm0]])' scene=''> | <StructureSection load=1iyt size='500' side='right' caption='amyloid-beta(1-42)', ([[1dm0]])' scene=''> | ||
==Introduction== | ==Introduction== | ||
'''Alzheimer's disease''' is characterized by extracellular proteic plaques and intracellular neurofibrillary tangles.<ref name="structure">PMID: 12423364</ref> These plaques are collections of fibrils consisting mostly of beta-amyloid fibrils. These fibril | '''Alzheimer's disease''' is characterized by extracellular proteic plaques and intracellular neurofibrillary tangles.<ref name="structure">PMID: 12423364</ref> These plaques are collections of fibrils consisting mostly of beta-amyloid <scene name='Amyloid_beta/Fibrils/1'>fibrils</scene>. These fibril are aggregates of beta-sheets though amyloid betam can also form alpha helices that create pores in the membrane that trigger cell death.<ref name="structure" /> | ||
'''Amyloids''' are insoluble fibrous proteins | '''Amyloids''' are insoluble fibrous proteins | ||
Revision as of 03:58, 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.[1] These plaques are collections of fibrils consisting mostly of beta-amyloid . These fibril are aggregates of beta-sheets though amyloid betam can also form alpha helices that create pores in the membrane that trigger cell death.[1] 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]