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

Lingling Xu; Marie Laurence Tremblay; Qing Meng; Xiang Qin Liu; Jan K. Rainey

doi:10.1007/s12104-011-9344-z

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

Lingling Xu, Marie Laurence Tremblay, Qing Meng, Xiang Qin Liu, Jan K. Rainey

Medicine

Résultat de recherche: Article › examen par les pairs

23 Citations (Scopus)

Résumé

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.

Langue d'origine	English
Pages (de-à)	147-151
Nombre de pages	5
Journal	Biomolecular NMR Assignments
Volume	6
Numéro de publication	2
DOI	https://doi.org/10.1007/s12104-011-9344-z
Statut de publication	Published - oct. 2012

Note bibliographique

Funding Information:
Fig. 3 Chemical shift index (CSI, Wishart et al. 1992) histogram illustrating the predicted secondary structures of W1 according Hα, Cα, Cβ, and C′. The CSI plot and DANGLE secondary structure prediction was generated by Analysis (Vranken et al. 2005; Cheung et al. 2010). The stars above certain bars indicate deviations greater then the range shown. Refer to Fig. 1 for the protein sequence and respective numbering of amino acids 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.

ASJC Scopus Subject Areas

Structural Biology
Biochemistry

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10.1007/s12104-011-9344-z

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

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.",

author = "Lingling Xu and Tremblay, {Marie Laurence} and Qing Meng and Liu, {Xiang Qin} and Rainey, {Jan K.}",

note = "Funding Information: Fig. 3 Chemical shift index (CSI, Wishart et al. 1992) histogram illustrating the predicted secondary structures of W1 according Hα, Cα, Cβ, and C′. The CSI plot and DANGLE secondary structure prediction was generated by Analysis (Vranken et al. 2005; Cheung et al. 2010). The stars above certain bars indicate deviations greater then the range shown. Refer to Fig. 1 for the protein sequence and respective numbering of amino acids 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{\textquoteright}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 Qu{\'e}bec/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 Qu{\'e}bec minist{\`e}re 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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AU - Meng, Qing

AU - Liu, Xiang Qin

AU - Rainey, Jan K.

N1 - Funding Information: Fig. 3 Chemical shift index (CSI, Wishart et al. 1992) histogram illustrating the predicted secondary structures of W1 according Hα, Cα, Cβ, and C′. The CSI plot and DANGLE secondary structure prediction was generated by Analysis (Vranken et al. 2005; Cheung et al. 2010). The stars above certain bars indicate deviations greater then the range shown. Refer to Fig. 1 for the protein sequence and respective numbering of amino acids 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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