2H and 13C NMR studies on the temperature-dependent water and protein dynamics in hydrated elastin, myoglobin and collagen.

(2)H NMR spin-lattice relaxation and line-shape analyses are performed to study the temperature-dependent dynamics of water in the hydration shells of myoglobin, elastin, and collagen. The results show that the dynamical behaviors of the hydration waters are similar for these proteins when using comparable hydration levels of h=0.25-0.