By Ronald Wetzel, Indu Kheterpal
The facility of polypeptides to shape then again folded, polymeric buildings corresponding to amyloids and similar aggregates is being more and more well-known as an important new frontier in protein examine. This new quantity of tools 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 specified protocols and methodological insights, supplied by way of leaders within the box, into the most recent equipment for investigating the constructions, mechanisms of formation, and organic actions of this significant category of protein assemblies.
* offers precise protocols
* comprises troubleshooting information
* offers assurance on structural biology, computational equipment, and biology
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Extra info for Amyloid, Prions, and Other Protein Aggregates, Part C
This procedure, although somewhat cumbersome, provides excellent dust‐free samples. The peak volumes of different A fractions are large relative to the volume of the cuvette; therefore, the cuvette behaves analogously to the detector flow cell in that cross‐contamination among different fractions is not problematic. Acknowledgments This work was supported by grants NS38328, NS44147, AG18921, and AG027818 from the National Institutes of Health and by the Foundation for Neurologic Diseases. The author thanks Drs.
Determine the weight concentration of aggregates, if desired. Preserve the stock suspensions by snap‐freezing in dry ice and ethanol or liquid nitrogen and then placing the stocks at À80 for long‐term storage. 4. If desired, sonicate the aggregate stock suspension using a probe sonicator. We typically sonicate on ice five times using a cycle of a 30‐s pulse followed a by 1‐min delay. We normally include 1 mM DTT as a precaution against air oxidation during the sonication, but, of course, this is not advisable, for example, for mutated A fibrils containing disulfide bonds.
Jao, S. , and Zagorski, M. G. (1997). Trifluoroacetic acid pretreatment reproducibly disaggregates the amyloid peptide. Amyloid 4, 240–252. , Lashuel, H. , Hartley, D. , Lansbury, P. , and Wetzel, R. (2003). A protofibrils possess a stable core structure resistant to hydrogen exchange. Biochemistry 42, 14092–14098. , Cook, K. , and Wetzel, R. (2000). A amyloid fibrils possess a core structure highly resistant to hydrogen exchange. Proc. Natl. Acad. Sci. USA 97, 13597– 13601. 32 amyloid, prions, and other protein aggregates, part C  Kirkitadze, M.
Amyloid, Prions, and Other Protein Aggregates, Part C by Ronald Wetzel, Indu Kheterpal