Fig. 6: Addition of a Ca(II) chelator to the cTn complex provides insights into cTn-Ca(II) binding dynamics. | Nature Communications

Fig. 6: Addition of a Ca(II) chelator to the cTn complex provides insights into cTn-Ca(II) binding dynamics.

From: Structure and dynamics of endogenous cardiac troponin complex in human heart tissue captured by native nanoproteomics

Fig. 6

a Illustration of the cTn complex unfolding when incubated with increasing concentrations of EGTA; a Ca(II) ion chelator that sequesters cTn-bound Ca(II). b Mass spectrum of the cTn complex (z = 18-21+) by native TIMS-MS. c Associated ion mobility heat map corresponding to the data presented in (b). d Enriched cTn complex were incubated with 0, 25, 50, and 100 mM EGTA for 3h at 4 °C and then analyzed by native TIMS-MS. e Base peak mobilogram spectra (BPM) of cTn complex incubated with EGTA (z = 20+). f Collision cross section (CCS) analysis of cTn complex incubated with EGTA (z = 20+) obtained under N2 drift gas. The loss of protein complex stability directly correlates with increasing EGTA concentration (25 to 100 mM).

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