By Ronald Wetzel, Indu Kheterpal
The power of polypeptides to shape however folded, polymeric constructions reminiscent of amyloids and similar aggregates is being more and more well-known as a huge new frontier in protein examine. This new quantity of Methods 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 exact 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 classification of protein assemblies.
- Presents particular protocols
- Includes troubleshooting tips
- Provides insurance on structural biology, computational tools, and biology
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Extra resources for Amyloid Prions and Other Protein Aggregates
1992). Expression and characterization of full‐length and partial human androgen receptor fusion proteins. Implications for the production and applications of soluble steroid receptors in Escherichia coli. Mol. Cell. Endocrinol. 84, 1–14. , Bulgakov, O. , Scott, S. , and Dalton, J. T. (2001). Recombinant expression and purification of human androgen receptor in a baculovirus system. Biochem. Biophys. Res. Commun. 284, 828–835. , and Wilson, E. M. (1999). Redox‐dependent DNA binding of the purified androgen receptor: Evidence for disulfide‐linked androgen receptor dimers.
2004c). Structural and functional analysis of the Josephin domain of the polyglutamine protein ataxin‐3. Biochem. Biophys. Res. Commun. 322, 387–394. Chow, M. , Paulson, H. , and Bottomley, S. P. (2004d). Destabilization of a non‐ pathological variant of ataxin‐3 results in fibrillogenesis via a partially folded intermediate: A model for misfolding in polyglutamine disease. J. Mol. Biol. 335, 333–341. Davies, S. , and Bates, G. P. (1998). Are neuronal intranuclear inclusions the common neuropathology of triplet‐repeat disorders with polyglutamine‐repeat expansions?
1999, 2005). Protein solutions of exceptional clarity (particulate‐free) are required if such techniques are to be used successfully. A ‘‘magic formula’’ for manipulating A does not exist. , 2004) to solubilize and disaggregate A lyophilizates. For example, examination of the secondary structure of A dissolved in neat DMSO revealed no ‐sheet (Shen and Murphy, 1995). 1% TFA in acetonitrile (Shen and Murphy, 1995). 1%) TFA concentrations were not effective in disaggregating A or preventing its self‐association.