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 debined and has an RMSD of 0.38 angstroms while the second (residues 28-38) is interrupted at the Ile32-Gly33 connection connected by a kink (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 00:20, 26 November 2011

<StructureSection load=1iyt size='500' side='right' caption='amyloid-beta(1-42)', (1dm0)' scene=>

IntroductionIntroduction

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).

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Laura Olney, Michal Harel, Alexander Berchansky