Well-defined, fluorescence-free Raman spectra were obtained from native as
well as treated (supercontracted) major ampullate dragline silks reeled fro
m four very different spiders: Araneus diadematus, Nephila edulis, Latrodec
tus mactans and Euprosthenops sp. Conformational sensitive regions were ass
igned in the spectra. Compared to the silk of the silkworm Bombyx mori, all
spider silks showed less beta-sheet and more random coil and/or alpha-heli
x material. Polarized spectra suggested that the molecular chains of the sp
ider silk were aligned parallel to the axis of the fibre. The differences i
n the mechanical properties between the native and supercontracted silks we
re attributed to variations in beta-sheet content. The mechanism of contrac
tion of spider silks in solvents was correlated to conformational changes i
n the supermolecular structure. (C) 1999 Elsevier Science Ltd. All rights r
eserved.