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1H, 13C and 15N NMR assignments of the aciniform spidroin (AcSp1) repetitive domain of Argiope trifasciata wrapping silk

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Abstract

Spider silk is one of nature’s most remarkable biomaterials due to extraordinary strength and toughness not found in today’s synthetic materials. Of the seven types of silk, wrapping silk (AcSp1) is the most extensible of the types of silks and has no sequence similarity to the other types. Here we report the chemical shifts for the AcSp1 199 amino acid protein repeat unit and its anticipated secondary structure based on secondary chemical shifts.

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Acknowledgments

We thank Yanfei Wang for technical support in the gene preparation. This work was supported by a research grant from the Canadian Institutes of Health research to XQL; a Discovery Grant from the Natural Sciences and Engineering Research Council of Canada to JKR; research grants to QM from the National High Technology Research and Development Program 863 (NO 2006AA03Z451), the National Natural Science Foundation of China (NO 31070698), and the Shanghai key projects of basic research (NO 10JC1400300); and, a Nova Scotia Health Research Foundation Studentship Award to MLT. 700 MHz NMR data were collected at the Biomolecular Magnetic Resonance Facility (BMRF) housed at the National Research Council of Canada’s Institute for Marine Biosciences (NRC-IMB), as facilitated by the Nuclear Magnetic Resonance Research Resource (NMR-3). The He-cooled probe for the 700 MHz at the NRC-IMB was provided by Dalhousie University through an Atlantic Canada Opportunities Agency Grant. 500 MHz NMR experiments were recorded at the Québec/Eastern Canada High Field NMR Facility (QANUC), supported by grants from the Canada Foundation for Innovation, the Natural Sciences and Engineering Research Council of Canada, the Québec ministère de la recherche en science et technologie, and McGill University. Thanks to Dr. Tara Sprules for her expert data acquisition at QANUC.

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Authors and Affiliations

  1. Institute of Biological Sciences and Biotechnology, Donghua University, Shanghai, People’s Republic of China

    Lingling Xu & Qing Meng

  2. Department of Biochemistry & Molecular Biology, Dalhousie University, Halifax, NS, B3H 4R2, Canada

    Lingling Xu, Marie-Laurence Tremblay, Xiang-Qin Liu & Jan K. Rainey

  3. Department of Chemistry, Dalhousie University, Halifax, NS, B3H 4R2, Canada

    Jan K. Rainey

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  1. Lingling Xu
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  2. Marie-Laurence Tremblay
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  3. Qing Meng
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  4. Xiang-Qin Liu
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Correspondence to Xiang-Qin Liu or Jan K. Rainey.

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Lingling Xu and Marie-Laurence Tremblay contributed equally.

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Xu, L., Tremblay, ML., Meng, Q. et al. 1H, 13C and 15N NMR assignments of the aciniform spidroin (AcSp1) repetitive domain of Argiope trifasciata wrapping silk. Biomol NMR Assign 6, 147–151 (2012). https://doi.org/10.1007/s12104-011-9344-z

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  • DOI: https://doi.org/10.1007/s12104-011-9344-z

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