Super Spy Variants Implicate Flexibility in Chaperone Action

Quan S, et al., 3:e01584, Elife, 2014

Genetic screening was performed to isolate variants of the Spy chaperone that better stabilize poorly folded protein clients and prevent degradation in vivo while also having an improved ability to prevent aggregation of proteins in vitro. Termed "super-Spy", the isolated variants examined in binding studies using the Octet RED system clearly demonstrated a stronger affinity to client proteins than the WT form and provided insight into better understanding chaperone function and protein degradation. Streptavidin biosensors were used.

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