Table 1.
Protein | Mass (Obs) | Mass (calc) | Elution time (min) | CD (222 nm) | Gnd-midpoint | ΔG (kcal/mole) |
n86 | 8625.9 | 8627.7 | nd | −21,950 | 1.7 M | 3.0 |
S-23 | 11856.0 | 11855.2 | 23.35 | −25,890 | 3.7 M | 6.6 |
S-213 | 11857.0 | 11856.3 | 23.35 | −29,690 | 3.4 M | 8.4 |
S-285 | 12063.2 | 12062.5 | 23.79 | −32,870 | 3.6 M | 9.5 |
S-824 | 11928.8 | 11928.4 | 23.77 | −29,710 | 3.2 M | 7.7 |
S-836 | 11927.7 | 11927.4 | 23.76 | −31,550 | 3.0 M | 5.4 |
cyt C | 12384 | 22.60 |
Mass (obs) was measured using electrospray mass spectrometry. Mass (calc) was calculated from the sequences. Elution times were measured using size-exclusion chromatography performed at the same concentrations as NMR experiments. CD (222 nm) indicates mean residue ellipticity at 222 nm at 20°C. Gnd midpoint is the concentration of guanidine hydrochloride at which 50% of the protein sample is denatured. ΔG indicates the free energy of unfolding in the absence of denaturant, and is derived by extrapolation of the guanidine denaturation data.