1H and 2H NMR Relaxation Studies of a High Mr Subunit of Wheat Glutenin and Comparison with Elastin

Abstract

The NMR-relaxation properties of a high Mr (HMW) subunit of wheat glutenin were studied using 1H and 2H resonance. 1 H transverse relaxation measurements were made on dry and D2O hydrated samples (20-80% protein; w/w). 2H transverse relaxation experiments on the hydrated (20 and 33% protein; w/w) high Mr subunit between 298 and 363 K indicated that the relaxation component associated with free D2O decreased in proportion with increasing temperature. This behaviour is different from that reported previously for mammalian elastin. It shows that the high Mr subunits of glutenin are not elastin-like in their interaction with water. The experiments failed to support a previous proposal that a similarity may exist between the mechanism of elasticity in elastin and in high Mr subunits.