Exploring the amyloid state of proteins by micro

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caView down the fibril axis shows selfcomplementaryinteractions betweenpaired beta sheets of the steric zipperand weak interactions between pairsOne unit cellNelson et al. Nature, 2005Nine unit cells
As of April 2011, ~90 X-raycrystal structures of fibrillikedry steric zippers from12 disease-relatedproteins:Sup35 and PrP prionsAβ and Tau - Alzheimer’sα-synuclein - Parkinson’sIAPP - Diabetes type 2SOD - ALSTransthyritin-familialamyloidosisLysozyme-lysozymeamyloidosisInsulin-injectionamyloidosisSEVI-HIV transmission
Page 1 and 2: The Amyloid State of Proteinsand Mi
Page 3 and 4: Amyloid• Unbranched, elongated pr
Page 5 and 6: My Scientific Dilemma in 2001Import
Page 7 and 8: 10-100 mM < 24 hrGNNQQNY microcryst
Page 9 and 10: Packing of GNNQQNY peptides in micr
Page 11 and 12: Microfocus is required to reducebac
Page 13: GNNQQNY, a dry steric zipperFibers
Page 17 and 18: D-TLKIVW prevents fibril formation
Page 19 and 20: GGVVIA +JugloneMeytal LandauGGVVIA
Page 21 and 22: Structure of KLVFFA with Orange GKL
Page 23 and 24: Amyloid-like crystalsof KLIMY from
Page 25 and 26: Nano-crystals oflonger (11-residue)
Page 27 and 28: 10 micron Mictigen micromesh in cry
Page 29 and 30: Drosophila crystal cellon 10 µm me
Page 31 and 32: Cell Types Containing Intracellular
Page 33 and 34: The Amyloid State of ProteinsUCLA:

Exploring the amyloid state of proteins by micro

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