Protein secondary structure of Green Lynx spider dragline silk investigated by solid-state NMR and X-ray diffraction》.pdf

International Journal of Biological Macromolecules 81 (2015) 171–179 Contents lists available at ScienceDirect International Journal of Biological Macromolecules j o u r na l h o me p a g e : w w w. elsev /locate/ijbiomac Protein secondary structure of Green Lynx spider dragline silk investigated by solid-state NMR and X-ray diffraction Dian Xu, Xiangyan Shi, Forrest Thompson, Warner S. Weber, Qiushi Mou, Jeffery L. Yarger ∗ Department of Chemistry and Biochemistry, Magnetic Resonance Research Center, Arizona State University, Tempe, AZ 85287-1604, United States a r t i c l e i n f o a b s t r a c t Article history: In this study, the secondary structure of the major ampullate silk from Peucetia viridans (Green Lynx) Received 12 May 2015 spiders is characterized by X-ray diffraction and solid-state NMR spectroscopy. From X-ray diffraction Received in revised form 23 July 2015 measurement, -sheet nanocrystallites were observed and found to be highly oriented along the fiber Accepted 24 July 2015 axis, with an orientational order,f c ≈ 0.98. The size of the nanocrystallites was determined to be on average Available online 29 July 2015 2.5 nm ×3.3 nm ×3.8 nm. Besides a prominent nanocrystalline region, a partially oriented amorphous region was also observed with an f a ≈ 0.89. Two-dimensional 13C–13C through-space and through-bond Keywords: solid-state NMR experiments were employed to elucidate structure details of P. virida