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. 2020 Jan 1;109(1):1–13. doi: 10.1016/j.xphs.2019.08.001

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© 2019 The Authors.

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Morphology and structural analysis of protein within aggregates/particles formed for P[8] antigen after shake stress in base buffer. (a) Representative particle images recorded by micro–flow imaging microscopy, (b) optical microscopic image of an isolated protein particle/aggregate, (c) secondary structure analysis of protein in isolated insoluble protein particles/aggregates by FTIR microscopy, (d) higher order structure integrity analysis of unstressed and stressed protein in the supernatant (S) and pellet (P) fractions by ANS fluorescence spectroscopy, and inter-molecular disulfide bond analysis of unstressed and stressed protein in S and P fractions by (e) nonreduced and (f) reduced SDS-PAGE (lane 1—S unstressed, lanes 2,3,4—S stressed, lane 5—MW marker, lane 6—P unstressed, and lanes 7,8,9—P stressed). (g) Relative solubility assessment of 3 NRRV antigens using ammonium sulfate precipitation assay, error bars represent 1SD from triplicate experiments.