Molecular Weight Effect on Secondary Structural Formation for Uniform Polypeptides with a Repeating Sequence of Glycine-Rich Sequence of Spider Dragline Silk
Polypeptides with a repeating sequence of glycine-rich sequence of spider dragline silk formed a β-sheet structure which exists in the crystalline region. The β-sheet content increased with increasing the molecular weight of the polypeptides. The formation of the β-sheet structure could be caused by the intramolecular as well as intermolecular conventional hydrogen bondings.