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1H, 13C and 15N NMR assignments of the aciniform spidroin (AcSp1) repetitive domain of Argiope trifasciata wrapping silk.
Biomol NMR Assign. 2012 Oct; 6(2):147-51.BN

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.

Authors+Show Affiliations

Institute of Biological Sciences and Biotechnology, Donghua University, Shanghai, People's Republic of China.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

21989955

Citation

Xu, Lingling, et al. "1H, 13C and 15N NMR Assignments of the Aciniform Spidroin (AcSp1) Repetitive Domain of Argiope Trifasciata Wrapping Silk." Biomolecular NMR Assignments, vol. 6, no. 2, 2012, pp. 147-51.
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. 2012;6(2):147-51.
Xu, L., Tremblay, M. L., Meng, Q., Liu, X. Q., & Rainey, J. K. (2012). 1H, 13C and 15N NMR assignments of the aciniform spidroin (AcSp1) repetitive domain of Argiope trifasciata wrapping silk. Biomolecular NMR Assignments, 6(2), 147-51. https://doi.org/10.1007/s12104-011-9344-z
Xu L, et al. 1H, 13C and 15N NMR Assignments of the Aciniform Spidroin (AcSp1) Repetitive Domain of Argiope Trifasciata Wrapping Silk. Biomol NMR Assign. 2012;6(2):147-51. PubMed PMID: 21989955.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - 1H, 13C and 15N NMR assignments of the aciniform spidroin (AcSp1) repetitive domain of Argiope trifasciata wrapping silk. AU - Xu,Lingling, AU - Tremblay,Marie-Laurence, AU - Meng,Qing, AU - Liu,Xiang-Qin, AU - Rainey,Jan K, Y1 - 2011/10/12/ PY - 2011/08/12/received PY - 2011/09/27/accepted PY - 2011/10/13/entrez PY - 2011/10/13/pubmed PY - 2013/2/1/medline SP - 147 EP - 51 JF - Biomolecular NMR assignments JO - Biomol NMR Assign VL - 6 IS - 2 N2 - 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. SN - 1874-270X UR - https://www.unboundmedicine.com/medline/citation/21989955/1H_13C_and_15N_NMR_assignments_of_the_aciniform_spidroin__AcSp1__repetitive_domain_of_Argiope_trifasciata_wrapping_silk_ L2 - https://dx.doi.org/10.1007/s12104-011-9344-z DB - PRIME DP - Unbound Medicine ER -