By Ronald Wetzel, Indu Kheterpal
The facility of polypeptides to shape then again folded, polymeric constructions similar to amyloids and similar aggregates is being more and more famous as an enormous new frontier in protein examine. This new quantity of tools in Enzymology besides half B (volume 412) 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 equipment for investigating the constructions, mechanisms of formation, and organic actions of this crucial category of protein assemblies.
* provides unique protocols
* contains troubleshooting assistance
* offers assurance on structural biology, computational equipment, and biology
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Additional info for Amyloid, Prions, and Other Protein Aggregates, Part C
Experimental Results The sedimentation assay requires a standard curve relating the integrated area of a peptide HPLC peak to the mass of the peptide. The assay requires reproducible recovery of injected peptide throughout the dynamic range of the assay and, preferably, nearly quantitative recovery. Wavelengths in the range of 215 to 220, where the peptide bond (and other amides) strongly absorb, are normally used for quantitation. Figure 3 shows the excellent linearity of response for A(1‐40) and for the peptide K2Q25K2 using peptide stock solutions that were independently calibrated for concentration using amino acid composition analysis.
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Chem. 276, 35176–35184. , and Teplow, D. (2005). Preparation of aggregate‐free, low molecular weight amyloid‐ for assembly and toxicity assays. In ‘‘Amyloid Proteins—Methods and Protocols’’ (D. E. M. ), pp. 3–9. Humana Press, Totowa, NJ. Buck, M. (1998). Trifiuoroethanol and colleagues: Cosolvents come of age. Recent studies with peptides and proteins. Q. Rev. Biophys. 31, 297–355. Buxbaum, J. N. (2003). Diseases of protein conformation: What do in vitro experiments tell us about in vivo diseases?
Amyloid, Prions, and Other Protein Aggregates, Part C by Ronald Wetzel, Indu Kheterpal