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. Author manuscript; available in PMC: 2022 May 18.
Published in final edited form as: FEBS J. 2020 May 26;288(2):678–698. doi: 10.1111/febs.15363

Fig. 9.

Fig. 9.

Tryptophan fluorescence quenching of pro-tPMII D214A mutant. (A) Quenching of fluorescence of pro-tPMII D214A in pH 7.5 and 5.0, with and without inhibitor; mature PMII and mature PMII D214A mutant are taken as positive controls. (B) Fluorescence quenching of pro-tPMII D214A mutant at pH 5.0 in the presence of PepA (0–10 μm). The experiments were performed in quintuplicate (n = 5), and the data are represented as a mean of all the measurements.