By Ronald Wetzel, Indu Kheterpal

The facility of polypeptides to shape however folded, polymeric constructions comparable to amyloids and comparable aggregates is being more and more well-known as an incredible 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 specified protocols and methodological insights, supplied through leaders within the box, into the newest tools for investigating the constructions, mechanisms of formation, and organic actions of this significant classification of protein assemblies.

* offers exact protocols
* contains troubleshooting advice
* offers insurance on structural biology, computational tools, and biology

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

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And Hong, A. (1999). Methodological and chemical factors affecting amyloid‐ peptide amyloidogenicity. Methods Enzymol. 309, 189–204. 34 amyloid, prions, and other protein aggregates, part C [3] [3] Kinetics and Thermodynamics of Amyloid Assembly Using a High‐Performance Liquid Chromatography–Based Sedimentation Assay By BRIAN O’NUALLAIN, ASHWANI K. THAKUR, ANGELA D. WILLIAMS, ANUSRI M. BHATTACHARYYA, SONGMING CHEN, GEETHA THIAGARAJAN , and RONALD WETZEL Abstract Nonnative protein aggregation has been classically treated as an amorphous process occurring by colloidal coagulation kinetics and proceeding to an essentially irreversible endpoint often ascribed to a chaotic tangle of unfolded chains.

Solution NMR studies of the A (1‐40) and A (1‐42) peptides establish that the Met35 oxidation state affects the mechanism of amyloid formation. J. Am. Chem. Soc. 126, 1992–2005. Howlett, D. , Jennings, K. , Lee, D. , Clark, M. , Wood, S. , and Roberts, G. W. (1995). Aggregation state and neurotoxic properties of Alzheimer ‐amyloid peptide. Neurodegeneration 4, 23–32. Huang, T. , Yang, D. , Plaskos, N. , Yip, C. , Fraser, P. , and Chakrabartty, A. (2000). Structural studies of soluble oligomers of the Alzheimer ‐amyloid peptide.

Sci. USA 97, 13597– 13601. 32 amyloid, prions, and other protein aggregates, part C [2] Kirkitadze, M. , and Teplow, D. B. (2002). Paradigm shifts in Alzheimer’s disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies. J. Neurosci. Res. 69, 567–577. Klein, W. , Stine, W. , and Teplow, D. B. (2004). Small assemblies of unmodified amyloid ‐protein are the proximate neurotoxin in Alzheimer’s disease. Neurobiol. Aging 25, 569–580. Krakow, N. P. (1898). Beitdige zur chemie der amyloidenartung.

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