Luedtke NW, Dexter RJ, Fried DB, Schepartz A. Surveying polypeptide and protein domain conformation and association with FlAsH and ReAsH. Nat Chem Biol. 2007 Nov 4;

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  1. This exciting study describes a novel method for detecting the misfolding of proteins in live cells using the FlAsH system. By splitting the bipartite tetracysteine motif required for FlAsH fluorescence between distant locations in the amino acid sequence of a protein that are only brought into close proximity by correct folding, the authors are able to use the FlAsH dye to detect whether proteins fold correctly or not, even in live cell culture. This work is of great potential significance to those working on diseases associated with protein misfolding, as the ability to detect misfolding events occurring in situ in live cells has the potential to transform our understanding of the dynamics of such events and how they relate to cellular toxicity. Furthermore, by demonstrating the ability of this system to detect protein-protein interactions, this work offers the tempting possibility of being able to use this approach to study, directly and in detail, protein aggregation phenomena in a cellular environment.

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