Download Amyloid, Prions, and Other Protein Aggregates, Part C by Ronald Wetzel, Indu Kheterpal PDF

By Ronald Wetzel, Indu Kheterpal

The power of polypeptides to shape on the other hand folded, polymeric buildings comparable to amyloids and similar aggregates is being more and more famous 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 most recent tools for investigating the buildings, mechanisms of formation, and organic actions of this significant type of protein assemblies.

* provides distinct protocols
* contains troubleshooting suggestions
* offers assurance on structural biology, computational equipment, and biology

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

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Fraser, P. , and Chakrabartty, A. (2000). Structural studies of soluble oligomers of the Alzheimer ‐amyloid peptide. J. Mol. Biol. 297, 73–87. 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.

Soluble multimeric Alzheimer (1‐40) pre‐amyloid complexes in dilute solution. Neurobiol. Aging 16, 755–764. , III. (2004). Alzheimer’s ‐peptide oligomer formation at physiologic concentrations. Anal. Biochem. 335, 81–90. , Benedek, G. , and Teplow, D. B. (1999). Monitoring protein assembly using quasielastic light scattering spectroscopy. Methods Enzymol. 309, 429–459. , Chung, D. , Benedek, G. , Kirschner, D. , and Teplow, D. B. (1996). On the nucleation and growth of amyloid ‐protein fibrils: Detection of nuclei and quantitation of rate constants.

45, 373–379. , Castano, E. , Kumar, R. , Beavis, R. , 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.

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