By Gal Bitan, David B. Teplow (auth.), Einar M. Sigurdsson (eds.)
A confirmed selection of conveniently reproducible recommendations for learning amyloid proteins and their involvement within the etiology, pathogenesis, prognosis, and treatment of amyloid illnesses. The individuals supply tools for the guidance of amyloid and its precursors (oligomers and protofibrils), in vitro assays and analytical ideas for his or her examine, and phone tradition versions and assays for the construction of amyloid proteins. extra chapters current comfortably reproducible concepts for amyloid extraction from tissue, its detection in vitro and in vivo, in addition to nontransgenic tools for constructing amyloid mouse versions. The protocols stick to the winning tools in Molecular Biology™ sequence layout, every one providing step by step laboratory directions, an creation outlining the main at the back of the procedure, lists of the mandatory apparatus and reagents, and pointers on troubleshooting and warding off recognized pitfalls.
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Additional resources for Amyloid Proteins: Methods and Protocols
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Purified AbARC protofibrils formed in the presence of WT are stable for 1 to 4 d at 4°C (as judged by SEC and EM) (12), providing sufficient time to study and characterize these intermediates. Therefore, a 1:1 mixture of AbARC and AbWT (100 µM) is used to prepare annular protofibrils of AbARC (Fig. 2). Attempts to separate Ab protofibrils prepared from Ab40 or Ab40ARC alone on superose 6 have failed, as the protofibrils have been observed to interact with the column matrix and/or undergo dissociation to monomers.
Some peptides from the tau sequence can adopt a-helical conformation, but only in non-physiological buffers including helix-inducing agents (12–15). Earlier studies on tau in PHFs using X-ray fiber diagrams of NFTs or reassembled tau fibers show only weak or no contributions from b-structure (11,16). Additionally, neurofibrillary tangles and tau fibers stain poorly with Congo red, a dye considered indicative of cross-b-structure, compared with thioflavin-S Purification of Tau 37 (17). Only recently, it was shown that upon polymerization of tau to PHFs a shift from a random coil structure to an increased b-structure content occurs (18–22).