Molecular modeling of unusual spiral structure in elastomeric wheat seed protein

The structure of the central repetitive domain of the high molecular weight glutenin subunits, a group of elastomeric proteins from the seeds of wheat, were modeled using structure prediction and molecular dynamics. Models were generated with spiral structures, based on repetitive β-reverse turns, within and spanning the repeat motifs of the central domains. The models were consistent with available data from biophysical studies on the intact proteins and spectroscopic (infra-red and nuclear magnetic resonance) studies of synthetic peptides.