AHSA2

AHSA2's interaction with cofactors or metal ions could potentially alter its binding affinity for Hsp90 or ATP, impacting its chemical role in modulating protein folding processes.

AHSA2's ATPase activity can be assessed using methods like enzyme-linked ATPase assays or radioactive ATP hydrolysis assays.

AHSA2's involvement in protein folding could impact disulfide bond formation and reduction, affecting the redox chemistry of the folding process and cellular redox homeostasis.

AHSA2's function in protein folding could be relevant to diseases like neurodegenerative disorders, where protein misfolding contributes to pathology.

AHSA2 assists Hsp90 in refolding denatured or misfolded proteins, contributing to cellular protein quality control.

Post-translational modifications like phosphorylation may influence AHSA2's interactions with Hsp90 and client proteins, impacting its folding assistance.

AHSA2 contributes to the cellular stress response by aiding in the refolding of denatured proteins, promoting cell survival under adverse conditions.

Researchers commonly use methods like siRNA-mediated knockdown or gene overexpression through transfection to modulate AHSA2 expression for functional studies.

AHSA2 facilitates proper conformational changes in Hsp90, enhancing its ability to interact with and stabilize client proteins involved in cell signaling.

AHSA2's interaction with Hsp90 involves specific chemical interactions. Rational design of small molecules targeting these interactions could potentially modulate AHSA2's function and impact protein folding pathways.