By Ronald Wetzel, Indu Kheterpal
The facility of polypeptides to shape on the other hand folded, polymeric constructions equivalent to amyloids and comparable aggregates is being more and more famous 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 particular 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 significant type of protein assemblies. * provides designated protocols* contains troubleshooting tips* offers insurance on structural biology, computational equipment, and biology
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Additional info for Amyloid, prions, and other protein aggregates, Part B
2004). , 2002) cause toxic effects associated with Alzheimer’s disease (Selkoe, 2004). , 2004). These protein structures are more METHODS IN ENZYMOLOGY, VOL. 412 Copyright 2006, Elsevier Inc. All rights reserved. , and Roda, A. (2005). Field‐flow fractionation and biotechnology. Trends Biotechnol. 23, 475–483. , Padgett, M. , Gajdusek, D. , and Gibbs, C. , Jr. (1990). Molecular mass, biochemical composition, and physicochemical behavior of the infectious form of the scrapie precursor protein monomer.
Conclusion The FFF family of techniques is capable of high‐resolution separations over an extremely large range of particle sizes (1 nm–100 m), all in the absence of a stationary phase. Thus, FFF is uniquely suited to accomplish separations of amyloid and other large bioparticles that have typically presented a challenge to some of the more traditional sizing methods found in biomedical laboratories. , 2005). In this era in which questions abound regarding the relationship between particle size and pathological activities of various abnormal protein aggregates, we suspect that FFF would also be highly applicable to studies of many important protein‐misfolding diseases.
Species‐barrier‐independent prion replication in apparently resistant species. Proc. Natl. Acad. Sci. USA 97, 10248–10253. Kascsak, R. , and Carp, R. I. (1991). Evidence for biological and structural diversity among scrapie strains. Curr. Top. Microbiol. Immunol. 172, 139–152. Kelly, J. W. (1998). The alternative conformations of amyloidogenic proteins and their multi‐ step assembly pathways. Curr. Opin. Struct. Biol. 8, 101–106. Kocisko, D. , Come, J. , Priola, S. , Raymond, G. , Lansbury, P. , and Caughey, B.
Amyloid, prions, and other protein aggregates, Part B by Ronald Wetzel, Indu Kheterpal