Silk materials have been the focus of renewed attention because they exhibit extraordinary mechanical strength and toughness.Two main factors are critical for understanding silks: the nanoscale semi crystalline folding structure, which gives high strength and exceptional toughness and the degree of hydration, which acts to modify these properties. Understanding and controlling these factors are the key to the functionality of protein elastomers. Silk fibroin is an ideal choice for (bio)material design-study and to probe H2O effects on protein dynamics, its interaction with and role in denaturation of proteins. The key molecular interactions are hydrogen bonds, one of the weakest chemical bonds known. Using a novel method to adjust the H2O content in situ with unprecedented accuracy and precision we aim to investigate effects of hydration on the protein torsional and vibrational dynamics.