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.
authors: Institute of Biological Sciences and Biotechnology, Donghua University, Shanghai, People's Republic of China.
authors: Lingling
authors: L
authors: Xu
authors: Marie-Laurence
authors: ML
authors: Tremblay
authors: Qing
authors: Q
authors: Meng
authors: Xiang-Qin
authors: XQ
authors: Liu
authors: Jan K
authors: JK
authors: Rainey
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002247:Carbon Isotopes; D005349:Fibroins / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D011522:Protons; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D020449:Repetitive Sequences, Amino Acid; D013112:Spiders / Q000737:chemistry*
chemical_list: D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D011522:Protons; D011993:Recombinant Fusion Proteins; D005349:Fibroins