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. Author manuscript; available in PMC: 2011 Apr 16.
Published in final edited form as: J Mol Biol. 2010 Feb 22;397(5):1307–1315. doi: 10.1016/j.jmb.2010.02.028

Fig. 3.

Fig. 3

P58(IPK) TPR domain I retains the full molecular chaperone acitvity.

An in vitro ELISA assay was performed to measure the direct binding between P58(IPK) TPR fragment (or its mutant) and the misfolded or native Luciferase (See methods). Denatured or native Luciferase was incubated in the presence of wild type P58(IPK) TPR fragment (residue 33–393, containing domain I, II and III), domain I+II (residue 33–267) or domain I (residue 33–168). The binding between Luciferase and P58(IPK) was monitored by ELISA. The readings are the averaged values of six independent experiments. Hamster Bip with 1mM ATP was used as a positive control.