H-1 AND H-2 NMR RELAXATION STUDIES OF A HIGH M(R) SUBUNIT OF WHEAT GLUTENIN AND COMPARISON WITH ELASTIN

The NMR-relaxation properties of a high M(r) (HMW) subunit of wheat gl utenin were studied using H-1 and H-2 resonance. H-1 transverse relaxa tion measurements were made on dry and D2O hydrated samples (20-80% pr otein; w/w). H-2 transverse relaxation experiments on the hydrated (20 and 33% protein; w/w) high M(r) subunit between 298 and 363 K indicat ed that the relaxation component associated with free D2O decreased in proportion with increasing temperature. This behaviour is different f rom that reported previously for mammalian elastin. It shows that the high M(r) subunits of glutenin are not elastin-like in their interacti on with water. The experiments failed to support a previous proposal t hat a similarity may exist between the mechanism of elasticity in elas tin and in high M(r) subunits.