TY - JOUR
T1 - Protein secondary structure of Green Lynx spider dragline silk investigated by solid-state NMR and X-ray diffraction
AU - Xu, Dian
AU - Shi, Xiangyan
AU - Thompson, Forrest
AU - Weber, Warner S.
AU - Mou, Qiushi
AU - Yarger, Jeffery
N1 - Publisher Copyright:
© 2015 Elsevier B.V.
PY - 2015/11/1
Y1 - 2015/11/1
N2 - In this study, the secondary structure of the major ampullate silk from Peucetia viridans (Green Lynx) spiders is characterized by X-ray diffraction and solid-state NMR spectroscopy. From X-ray diffraction measurement, β-sheet nanocrystallites were observed and found to be highly oriented along the fiber axis, with an orientational order, fc≈0.98. The size of the nanocrystallites was determined to be on average 2.5nm×3.3nm×3.8nm. Besides a prominent nanocrystalline region, a partially oriented amorphous region was also observed with an fa≈0.89. Two-dimensional 13C-13C through-space and through-bond solid-state NMR experiments were employed to elucidate structure details of P. viridans silk proteins. It reveals that β-sheet nanocrystallites constitutes 40.0±1.2% of the protein and are dominated by alanine-rich repetitive motifs. Furthermore, based upon the NMR data, 18±1% of alanine, 60±2% glycine and 54±2% serine are incorporated into helical conformations.
AB - In this study, the secondary structure of the major ampullate silk from Peucetia viridans (Green Lynx) spiders is characterized by X-ray diffraction and solid-state NMR spectroscopy. From X-ray diffraction measurement, β-sheet nanocrystallites were observed and found to be highly oriented along the fiber axis, with an orientational order, fc≈0.98. The size of the nanocrystallites was determined to be on average 2.5nm×3.3nm×3.8nm. Besides a prominent nanocrystalline region, a partially oriented amorphous region was also observed with an fa≈0.89. Two-dimensional 13C-13C through-space and through-bond solid-state NMR experiments were employed to elucidate structure details of P. viridans silk proteins. It reveals that β-sheet nanocrystallites constitutes 40.0±1.2% of the protein and are dominated by alanine-rich repetitive motifs. Furthermore, based upon the NMR data, 18±1% of alanine, 60±2% glycine and 54±2% serine are incorporated into helical conformations.
KW - Green Lynx
KW - Peucetia viridans
KW - Solid-state NMR
KW - Spider silk
KW - Wide-angle X-ray diffraction
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U2 - 10.1016/j.ijbiomac.2015.07.048
DO - 10.1016/j.ijbiomac.2015.07.048
M3 - Article
C2 - 26226457
AN - SCOPUS:84938888276
SN - 0141-8130
VL - 81
SP - 171
EP - 179
JO - International Journal of Biological Macromolecules
JF - International Journal of Biological Macromolecules
ER -