Amyloid structured

Pickersgill, R. W. (2003). A primordial structure underlying amyloid. Structure (Camb.) 11, 137-138. 

Fandrich, M., and Dobson, C. M. (2002). The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation. EMBOJ. 21, 5682-5690. Fandrich, M., Fletcher, M. A., and Dobson, C. M. (2001). Amyloid fibrils from muscle myoglobin. Nature 410, 165-166. 

Stabo-Eeg F, Lindgren M, Nilsson KPR, Inganas O, Hammarstrdm P (2007) Quantum efficiency and two-photon absorption cross-section of conjugated polyelectrolytes used for protein conformation measurements with applications on amyloid structures. Chem Phys 336 121-126... 

Modifications introduced by the mutations were central to the alteration of the specificities of the enzymes studied, which were capable of cleaving (3-casein at many new sites, for example, hydrolyzing the fragment Argl-Lysl05, reported to be a trypsin inhibitor (Bouhallab et al, 1997). Since many tryptic inhibitors contain amidated Glu and Asp, and form amyloid structures, the mutants of this type could be used for the hydrolysis of the lytically resistant protein structures. 

Fandrich M, Dobson CM (2002) The behavior of polyamino acids reveals an inverse side chain effect in amyloid structure formation. EMBO J 21 5682-5690... 

Our results are in complete accord with the suggestion that amyloid structures may arise from the generic properties of the proteins, with the details of the amino-acid side chains playing a secondary role. However, our work suggests that instead of an inverse side chain effect in amyloid structure formation [63], there is a unifying theme in the behavior of proteins. Just as the class of cross-linked [3-structures... 

The fluorescence excitation spectrum of the Thioflavin T (ThT, Sigma, Jerusalem, Israel) shifts from 340 to 450 run when interacting with (3-sheet amyloid structures (Levine, 1993, 1999). Fluorescence signals (excitation, 450 run emission, 485 nm) reflect the amount of amyloid fibrils formed. 

Sun Y, Breydo L, Makarava N, Yang Q, Bocharova OV, Baskakov IV (2007) Site-specific conformational studies of prion protein (PrP) amyloid fibrils revealed two cooperative folding domains within amyloid structure. J Biol Chem 282 9090-9097... 

However, overexpression ofYdjlp, a member of the Hsp40 family (Lu and Cyr, 1998), does cure [URE3] (Moriyama et al., 2000). These results suggest that many (perhaps all) prions are affected by chaperones, but the details may depend on the detailed properdes of the individual amyloid structures. 

Chatani, E., Kato, M Kawai, T., Naiki, H. Goto, Y. Main-chain dominated amyloid structures demonstrated by the effect of high pressure, J. Mol. Biol. 352 (2005) 941-951. 

Elliot et al. 2003). Previously shown to produce fibrils, chaplin from S. coelicolor can bind thiofiavin T (Claessen et al. 2003), suggesting they too possess amyloid structure. 

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