Table 1. The in silico unfolding propensities agree with the propensities derived from the experimental free energies for 16 protein structures.

Protein	PDB	Fit Score	%Matching	%Mismatching	Mutations
T4 Lysozyme	2LZM	0.156	78.6	21.4	84
Tyrosine-Protein Kinase	1FMK	0.241	71.4	28.6	49
Barnase	1BNI	0.245	72.7	27.3	140
Staphylococcal Nuclease	1STN	0.186	74.9	25.1	521
Protein L	1HZ6	0.152	75.4	24.6	57
Ribonuclease T1 Isozyme	1RN1	0.200	68.4	31.6	38
Gene V Protein	1VQB	0.254	69.6	30.4	92
Chymotrypsin Inhibitor 2	2CI2	0.157	78.2	21.8	78
Acyl-Coenzyme A	2ABD	0.199	83.9	16.1	31
Acylphosphatase	1APS	0.168	85.7	14.3	21
Alpha Spectrin	1AJ3	0.195	66.7	33.3	63
Dihydrofolate Reductase	1RX4	0.194	80.7	19.3	57
Ribosomal Protein S6	1RIS	0.094	100	0	16
Tryptophan Synthase	1WQ5	0.347	76.3	23.7	38
ARC Repressor	1ARR	0.230	70.1	29.9	77
Azurin	5AZU	0.085	93.1	6.9	29
Total					1,391

The unfolding propensities were calculated from the experimental ΔΔG values reported in the ProTherm database⁶¹. The percent matching values were calculated from the match matrices in Supplementary Material Table S1. The fit score was then calculated from the raw unfolding data. The fit score ranges from 0–1, with 1 being the worst fit and 0 being a perfect fit. The number of mutations for each analyzed protein was recorded in the last row to determine the total number of mutations compared.