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. | |||
'''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). | ||
Revision as of 21:31, 25 November 2011
<StructureSection load=1iyt size='500' side='right' caption='amyloid-beta(1-42)', (1dm0)' scene=>
Introduction
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 two helices; 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 kink (residues 26 and 27).
