~70μM: in the presence of stoichiometric amounts of the cochaperone Hsp40 ~50nM
||Theillet FX et al., Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs). Chem Rev. 2014 Jul 9 114(13):6661-714. doi: 10.1021/cr400695p p.6676 right column 4th paragraphPubMed ID24901537
|| Marie Couturier et al., High affinity binding between Hsp70 and the C‐terminal domain of the measles virus nucleoprotein requires an Hsp40 co‐chaperone. J. Mol. Recognit. 2009, 23, 301 link
||P.6676 right column 4th paragraph: "Another level of complexity may involve cochaperone interactions with both IDPs [intrinsically disordered proteins], and chaperones. The disordered C-terminal region of measles virus nucleoprotein for example, binds Hsp70 with ∼70 μM affinity (primary source) In the presence of stoichiometric amounts of the cochaperone Hsp40, the dissociation constant decreases to ∼50 nM. Thus, cochaperones can modulate IDP-chaperone affinities, which may be particularly important during translation, when multiple chaperones and cochaperones line the ribosomal exit tunnel (ref 369)."