By Ronald Wetzel, Indu Kheterpal
The facility of polypeptides to shape on the other hand folded, polymeric buildings resembling amyloids and similar aggregates is being more and more famous as a big new frontier in protein examine. This new quantity of Methods 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 exact 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 type of protein assemblies.
- Presents designated protocols
- Includes troubleshooting tips
- Provides insurance on structural biology, computational equipment, and biology
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Additional info for Amyloid Prions and Other Protein Aggregates
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. , 1997). , 1996; Zagorski and Barrow, 1992), leading to disruption of preexistent ‐sheet structure. , 2003). Preparing A for Biophysical and Biological Study In this section, I discuss the technique and benefits of pretreating synthetic A with NaOH.
7. 3. Lower incubation to temperature to 28 . 5 h. 4. Harvest cells by centrifugation at 6000g for 15 min at 4 . Resuspend cells in 40 ml lysis buffer, snap freeze, and store at À20 until purification. Purification of His6‐Tagged Ataxin‐3 Variants The method outlined below describes the purification of ataxin‐3 variants expressed with an N‐terminal His6 tag. This protocol has been used successfully for variants containing 15, 28, and 50 residues in the polyglutamine tract. Typical yields range between 5 and 10 mg of protein for 8 L of cells when purifying pQE‐His6‐Atax3 and between 10 and 20 mg of protein for 8 L of cells for pET‐His6‐Atax3.
Coli E. , 2003b E. coli E. coli E. , 2004 E. coli coli coli coli coli E. coli GST‐fusion (cleaved) No tag Q38 E. coli E. coli His6‐tagged Q38 GST‐fusion (cleaved) Q38 GST fusion (cleaved) Q23 His6‐tagged polyQ not stated E. , 1999 E. , 1999n Liao and Wilson, 2001o E. coli Chen, Y. , Allen, M. , Veprintsev, D. , and Bycroft, M. (2004). The structure of the AXH domain of spinocerebellar ataxin‐1. J. Biol. Chem. 279, 3758–3765. , and Pastore, A. (2003). The AXH module: An independently folded domain common to ataxin‐1 and HBP1.