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.