title: Structure-property relationships in major ampullate spider silk as deduced from polarized FTIR spectroscopy.
abstract: Polarized Fourier Transform Infrared (FTIR) spectroscopy is employed to study structure-property relationships in major ampullate spider silk being exposed to an external mechanical strain. From the measured infrared dichroism of aminoacid-residue - specific bands the molecular order parameter, the frequency width at half-maximum (FWHM) and the spectral position of the absorption maximum are determined in dependence on the external strain. For the highly ordered alanine-rich beta sheets a change in the vibrational potential is found for macroscopic strains as low as a few percent. It can be quantitatively described by a quantum-mechanical approach in which the mechanical strain is treated as a weak external perturbation. The immediate microscopic response to the external field proves that beta -sheeted crystals are tightly interconnected by pre-stretched chains as suggested recently (Y. Liu et al., Nat. Mater. 4, 901 (2005)).
authors.affiliation: Institut für Experimentelle Physik I, Universität Leipzig, Leipzig, Germany. papadopoulos@physik.uni-leipzig.de
authors.forename: P
authors.initials: P
authors.lastname: Papadopoulos
authors.forename: J
authors.initials: J
authors.lastname: Sölter
authors.forename: F
authors.initials: F
authors.lastname: Kremer
mesh_terms: D000818:Animals; D016880:Anisotropy; D003198:Computer Simulation; D004548:Elasticity; D054777:Hair Cells, Ampulla / Q000737:chemistry*; D008956:Models, Chemical; D008958:Models, Molecular; D011487:Protein Conformation; D047011:Silk / Q000737:chemistry* / Q000648:ultrastructure*; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods*; D013112:Spiders; D013314:Stress, Mechanical
chemical_list: D047011:Silk