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. Author manuscript; available in PMC: 2022 May 1.
Published in final edited form as: Mass Spectrom Rev. 2020 Jul 1;40(3):280–305. doi: 10.1002/mas.21642

FIGURE 16.

FIGURE 16.

(A) Melting curves for myohemerythrin (20 μM in 30 mM ammonium acetate, pH 6.8) show a unique unfolding and refolding pathway dictated by a structural rearrangement and formation of a non-native disulfide bond. Inset mass spectra show shifts towards higher charge and transition from holoprotein (filled circles) to apoprotein (open circles) with increasing temperature, followed by a shift towards lower charge state following the formation of the nonnative disulfide bond at high temperature. (B) Structures of the products formed by melting are shown along with respective CCS profiles and MS spectra. Reproduced from Woodall et al. (2019).