gonzalez - Solid State NMR Reveals a pH-dependent...

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Unformatted text preview: Solid State NMR Reveals a pH-dependent Antiparallel -Sheet Registry in Fibrils Formed by a -Amyloid Peptide A.T. Petkova, G. Buntkowsky, F. Dyda, R.D. Leapman, W.-M. Yau and R. Tycko Self-Propogating, Molecular-Level Polymorphism in Alzheimers -Amyloid Fibrils Anesta T. Petkova, Richard D. Leapman, Zhihong Guo, Wai-Ming Yau, Mark P. Mattson, Robert Tycko Victor M. Gonzalez Chemical Biology Tutorial September 21, 2005 Outline Background Amyloid Fibrils and disease Previous structural studies Solid-state NMR Petkova, et al Article 1 Petkova, et al Article 2 Conclusions Amyloid Fibrils Self-assembled filamentous clusters formed by different peptides and proteins. Distinguished by long -sheets with a cross- supramolecular structure Linked to various diseases, including Alzheimers and Huntingtons disease. Possible templates for nanomaterials Amyloid-Associated Diseases Amyloid Fibers play a role in disorders of protein metabolism. Normally soluble proteins and polypeptides are deposited in a fibrillar form in extracellular spaces. Accumulation leads to death. The development of amyloid deposits is linked to either genetic mutation, incorrect processing, or the abnormal accumulation of wild-type proteins Sunde and Blake, Q. Rev. Biophys. 31 , 1 (1998) Residues 11-25 of the -amyloid peptide are associated with Alzheimers Disease (AD)....
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This note was uploaded on 12/04/2011 for the course CHEM 590A taught by Professor Staff during the Summer '10 term at University of Illinois, Urbana Champaign.

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gonzalez - Solid State NMR Reveals a pH-dependent...

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