By Ronald Wetzel, Indu Kheterpal
The power of polypeptides to shape however folded, polymeric buildings akin to amyloids and similar aggregates is being more and more famous as an incredible 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 precise protocols and methodological insights, supplied by means of leaders within the box, into the newest tools for investigating the buildings, mechanisms of formation, and organic actions of this crucial classification of protein assemblies.
- Presents specified protocols
- Includes troubleshooting tips
- Provides assurance on structural biology, computational tools, and biology
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Additional resources for Amyloid Prions and Other Protein Aggregates
6 amyloid, prions, and other protein aggregates, part C  FIG. 1. Schematic representation of ataxin‐3 constructs. Purification is facilitated by the presence of the hexa‐histidine (His6) tag. In the second construct, the His6‐glutathione S‐transferase fusion partner is removed by tobacco etch virus (TEV) cleavage. FIG. 2. Construction of atax(Q50)/pQE30(EcoN1). (A) Schematic diagram of the atax3 (Q50)/pQE30(EcoN1) construct. The restriction enzyme recognition site for EcoN1 is shown at the right.
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.
The strategy involves sodium hydroxide pretreatment of synthetic A, followed by size fractionation procedures. This approach produces A solutions that have been used successfully in a variety of in vitro and in vivo experimental systems. Background A comprises the fibrils found in the senile plaques that are pathognomonic for AD (Selkoe, 1991). Genetic, physiological, and biochemical data support the hypothesis that A is a causative agent of AD (Selkoe, 2001). , 1991, 1993). , 1999), emphasizing the importance of a full elucidation of A assembly.