Amyloid, Prions, and Other Protein Aggregates, Part C by Ronald Wetzel, Indu Kheterpal

By Ronald Wetzel, Indu Kheterpal

The facility of polypeptides to shape however folded, polymeric constructions similar to amyloids and comparable aggregates is being more and more well-known as a huge new frontier in protein learn. This new quantity of equipment in Enzymology in addition to half B (volume 412) on Amyloid, Prions and different Protein Aggregates proceed within the culture of the 1st quantity (309) in containing particular protocols and methodological insights, supplied by means of leaders within the box, into the newest equipment for investigating the constructions, mechanisms of formation, and organic actions of this significant category of protein assemblies.

* provides special protocols
* contains troubleshooting counsel
* presents assurance on structural biology, computational equipment, and biology

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Extra info for Amyloid, Prions, and Other Protein Aggregates, Part C

Example text

It is recommended that one establish the appropriateness of the HPLC sedimentation assay as a faithful reporter of a reaction by carrying out a preliminary validation in which the aggregation reaction is monitored by multiple measures. Figure 4A shows the time course of a spontaneous aggregation reaction of a polyGln peptide as monitored by the sedimentation assay, the ThT assay, a Rayleigh light‐scattering assay, and CD monitoring of 50 amyloid, prions, and other protein aggregates, part C [3] FIG.

2002). Supramolecular structure in full‐length Alzheimer’s ‐amyloid fibrils: Evidence for a parallel ‐sheet organization from solid‐state nuclear magnetic resonance. Biophys. J. 83, 1205–1216. Barrow, C. , Kenny, P. T. , and Zagorski, M. (1992). Solution conformations and aggregational properties of synthetic amyloid peptides of Alzheimer’s disease. J. Mol. Biol. 225, 1075–1093. Benzinger, T. L. , Gregory, D. , Burkoth, T. , Lynn, D. , Botto, R. , and Meredith, S. C. (1998). Propagating structure of Alzheimer’s ‐amyloid(10–35) is parallel ‐sheet with residues in exact register.

Multiple quantum solid‐state NMR indicates a parallel, not anti parallel, organization of ‐sheets in Alzheimer’s ‐amyloid fibrils. Proc. Natl. Acad. Sci. USA 97, 13045–13050. Balbach, J. , Petkova, A. , Oyler, N. , Antzutkin, O. , Gordon, D. , Meredith, S. , and Tycko, R. (2002). Supramolecular structure in full‐length Alzheimer’s ‐amyloid fibrils: Evidence for a parallel ‐sheet organization from solid‐state nuclear magnetic resonance. Biophys. J. 83, 1205–1216. Barrow, C. , Kenny, P. T. , and Zagorski, M.

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