A39: Do Charged Residues in Grp94 Facilitate Client Binding: Insights into Chaperone Function

The Hsp90 family of chaperones functions to target misfolded proteins, prevent aggregate formation and bind to specific substrates for proper folding. Paralogs of the Hsp90 family exist in the cytoplasm (Hsp90), in the mitochondria (TRAP1) and in the endoplasmic reticulum (Grp94). The ER paralog Grp94 is of particular interest to this investigation since it is […]

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