By Ronald Wetzel, Indu Kheterpal
The facility of polypeptides to shape however folded, polymeric buildings similar to amyloids and comparable aggregates is being more and more famous as an incredible new frontier in protein learn. This new quantity of tools in Enzymology in addition to half C (volume 413) on Amyloid, Prions and different Protein Aggregates proceed within the culture of the 1st quantity (309) in containing special protocols and methodological insights, supplied by means of leaders within the box, into the newest tools for investigating the buildings, mechanisms of formation, and organic actions of this significant category of protein assemblies. * provides distinct protocols* contains troubleshooting advice* presents insurance on structural biology, computational equipment, and biology
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Extra info for Amyloid, prions, and other protein aggregates, Part B
FEBS Lett. 498, 204–207. Soto, C. (2004). Diagnosing prion diseases: Needs, challenges and hopes. Nat. Rev. Microbiol. 2, 809–819. , and Saborio, G. P. (2001). Prions: Disease propagation and disease therapy by conformational transmission. Trends Mol. Med. 7, 109–114. , Saborio, G. , and Anderes, L. (2002). Cyclic amplification of protein misfolding: Application to prion‐related disorders and beyond. Trends Neurosci. 25, 390–394. , Frossard, M. , Torres, J. , and Tagliavini, F. (2005). Pre‐symptomatic detection of prions by cyclic amplification of protein misfolding.
And Lansbury, P. , Jr. (1995). Aggregates of scrapie‐associated prion protein induce the cell‐free conversion of protease‐sensitive prion protein to the protease‐resistant state. Chem. Biol. 2, 807–817. , and Lansbury, P. T. (2003). Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26, 267–298. , Raymond, G. , Kocisko, D. , and Lansbury, P. , Jr. (1997). Scrapie infectivity correlates with converting activity, protease resistance, and aggregation of scrapie‐associated prion protein in guanidine denaturation studies.
5–1 mg/ml ($17–35 M) with the urea‐containing denaturing buffer. To trigger the polymerization reaction, we replace the denaturing  electrophoretic analysis of amyloids 43 buffer with the phosphate‐buffered saline solution using Micro Bio Spin 6 desalting columns (Bio‐Rad). Polymerization occurs spontaneously during rotation of the sample (60 rpm) at various temperatures for 48 h. To obtain a strong signal on the immunoblot, 1 g of Sup35NM per lane is enough. 5–2% (w/v) without affecting mobility of the polymers.
Amyloid, prions, and other protein aggregates, Part B by Ronald Wetzel, Indu Kheterpal