| Abstract Scope |
Proteins are the building blocks for some materials with outstanding mechanical properties, such as spider silk, which rivals the strength of steel. Given that interactions between protein molecules are only based on “weak” secondary interactions, such as hydrogen bonds and van der Waals forces, this is quite surprising. To understand this phenomenon, we have studied spider silk across the length scale with a plethora of experimental and computational techniques, including vibrational spectroscopy, nuclear magnetic resonance techniques, X-ray diffraction, as well as AFM imaging and force spectroscopy. We have developed a sophisticated multi-scale model of the structure and interactions between the different components of this hierarchical material, which has allowed us to establish a trace between molecular-scale interactions and macroscopic mechanical properties. This approach provides a deep understanding of existing materials and an assessment of the potential of future designer materials based on proteins and peptides. |