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 buildings equivalent to amyloids and comparable aggregates is being more and more well-known as an enormous new frontier in protein learn. 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 special protocols and methodological insights, supplied via leaders within the box, into the newest tools for investigating the buildings, mechanisms of formation, and organic actions of this significant classification of protein assemblies.

* provides distinctive protocols
* contains troubleshooting information
* offers assurance on structural biology, computational equipment, and biology

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

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Integrate the peak of the correct retention time, and obtain the micrograms of peptide from the standard curve. If automated software integration is used, it is best to confirm that it is giving appropriate numbers, especially as the signal‐to‐noise ratio decreases toward the end of the aggregation reaction, by manual integration. 5. Be vigilant for the time‐dependent appearance of new peaks in the HPLC assay that may indicate oxidation or hydrolysis of side chains in the peptide. Significant formation of chemical degradation products severely complicates kinetic and thermodynamic interpretations of the data.

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And Frangione, B. (1995). Fibrillogenesis of synthetic amyloid‐ peptides is dependent on their initial secondary structure. Neurosci. Lett. 200, 105–108. Stine, W. , Dahlgren, K. , Krafft, G. , and LaDu, M. J. (2003). In vitro characterization of conditions for amyloid‐ peptide oligomerization and fibrillogenesis. J. Biol. Chern. 278, 11612–11622. Taylor, B. , Sarver, R. , Poorman, R. , Lutzke, B. , Kappenman, A. , Buhl, A. , and Epps, D. E. (2003). Spontaneous aggregation and cytotoxicity of the ‐amyloid A 1–40: A kinetic model.

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