Amyloid, prions, and other protein aggregates, Part B by Ronald Wetzel, Indu Kheterpal

By Ronald Wetzel, Indu Kheterpal

The power of polypeptides to shape then again folded, polymeric buildings resembling amyloids and comparable aggregates is being more and more well-known as an important new frontier in protein examine. This new quantity of equipment in Enzymology besides half C (volume 413) 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. * offers special protocols* comprises troubleshooting counsel* offers assurance on structural biology, computational tools, and biology

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1. Customization of the transfer cassette from Mini‐Protean 2 transfer apparatus. Using a jigsaw, cut out the insert (C) from the cassette (A). Glue plastic spacers onto the frame (B) as shown (D). Glue the insert (C) onto D as shown. Repeat the procedure for the second half of the cassette (see text). [3] electrophoretic analysis of amyloids 39 charged protein–SDS complexes will migrate to the positive pole. It is important to ensure that the sandwich is not loose when the cassette is closed. If gels that are too thin are used, especially in combination with worn‐out sponges, insufficient or uneven tightness of the gel–membrane contact surface may lead to undirected transfer of the proteins and result in a faulty image, as shown in Fig.

2001). Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 411, 810–813. Saborio, G. , Kascsak, R. , Harris, D. , and Frangione, B. (1999). Cell‐lysate conversion of prion protein into its protease‐resistant isoform suggests the participation of a cellular chaperone. Biochem. Biophys. Res. Commun. 258, 470–475. Schiermeier, Q. (2001). Testing times for BSE. Nature 409, 658–659. [2] prion protein separation by FFF 21 Soto, C. (2001). Protein misfolding and disease; protein refolding and therapy.

Med. 7, 109–114. , Saborio, G. , and Anderes, L. (2002). Cyclic amplification of protein misfolding: Application to prion‐related disorders and beyond. Trends Neurosci. 25, 390–394. , Frossard, M. , Torres, J. , and Tagliavini, F. (2005). Pre‐symptomatic detection of prions by cyclic amplification of protein misfolding. FEBS Lett. 579, 638–642. Telling, G. , DeArmond, S. , and Prusiner, S. B. (1996). Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity.

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