By Ronald Wetzel, Indu Kheterpal
The power of polypeptides to shape on the other hand folded, polymeric constructions corresponding to amyloids and comparable aggregates is being more and more well-known as an immense new frontier in protein study. 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 specified protocols and methodological insights, supplied through leaders within the box, into the newest equipment for investigating the constructions, mechanisms of formation, and organic actions of this significant classification of protein assemblies.
* provides designated protocols
* contains troubleshooting information
* offers insurance on structural biology, computational tools, and biology
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Extra info for Amyloid, Prions, and Other Protein Aggregates, Part C
Glabe, C. , and Cotman, C. W. (1991). In vitro aging of ‐amyloid protein causes peptide aggregation and neurotoxicity. Brain Res. 563, 311–314. , and Franklin, E. C. (1969). Physical, chemical, and ultrastructural studies of water‐soluble human amyloid fibrils. J. Exp. Med. 130, 777–796. , and Dobeli, H. (1997). The toxicity of the Alzheimer’s ‐amyloid peptide correlates with a distinct fiber morphology. J. Struct. Biol. 119, 59–71. Selkoe, D. J. (1991). The molecular pathology of Alzheimer’s disease.
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. We have no data indicating that the DTT is required, but Met 35 of A is the most chemically labile amino acid residue in wild‐type A under most conditions.
USA 100, 330–335. , and Teplow, D. B. (2001). Amyloid ‐protein oligomerization— Prenucleation interactions revealed by photo‐induced crosslinking of unmodified proteins. J. Biol. 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.
Amyloid, Prions, and Other Protein Aggregates, Part C by Ronald Wetzel, Indu Kheterpal