Exploring the amyloid state of proteins by micro

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Microcrystals ofsegments of 15 amyloidformingproteins haveyielded >90 steric zippersX-ray beamCrystal50μGlass pin
GNNQQNY, a dry steric zipperFibers and microcrystal have 50,000 layersExtended strands, H-bonded 4.8Åapart into in register β-sheetsGln, Asn, Tyr sidechains also H-bondedTwo sheets, interdigitated, with tightlycomplementary sidechains, bondedby van der Waals forcesMore tightly complementary thanany previous structure in PDBDry between the β-sheetsNelson et al. Nature 2005
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: Microfocus is required to reducebac
Page 15 and 16: As of April 2011, ~90 X-raycrystal
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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