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Figure 1.4 Plots of the calculated monolayer hydration of globular proteins using the method of Miller and colleagues (1987a,b) to calculate the surface area of a theoretical fully hydrated protein (SASA max), a compact protein with surface-only hydration (SASA min), and an estimated native monolayer hydration with internal water molecules based on native collagen in tendon (Fullerton and Amurao, 2006). The hydration of hemoglobin measured by osmotic compression as shown in Fig. 1.9 agrees with this estimate.

(A2) and then converting to hydration fraction hmax = (1.48MW + 21)/ 8.59 x (18/MW) = 3.10 g/g independent of molecular weight as shown in Fig. 1.4. Thus the monolayer hydration of fully exposed collagen is identical to the average monolayer hydration of fully extended globular proteins over the entire range of molecular weights. Monolayer surface hydration of globular proteins is reduced, however, by folding to achieve a minimum free energy by removing as much hydrophobic surface as possible from exposure to water.

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