A: Experimental design to measure changes in thermal stability. Samples treated with either heat shock or mock shock are aliquot for treatment with temperatures that denature and aggregate all proteins. Samples are lysed with mild detergent (NP-40) and after tryptic digestion peptides from soluble protein fraction are labelled with TMT labels. The labelling is conducted so that samples from two adjacent temperature treatments are pooled and each TMT set is analyzed by mass spectrometer. At each temperature, the amount of protein still soluble is quantified and the fold change (FC) between heat shock and mock shock is calculated (see 'Materials and Methods' for details). Fold changes in each temperature are summed after adjustment for heat shock-induced aggregation. Fold change-based thermal stability measures are finally transformed to scores for thermal stability 