title: NMR assignments of the N-terminal domain of Nephila clavipes spidroin 1.
abstract: The building blocks of spider dragline silk are two fibrous proteins secreted from the major ampullate gland named spidroins 1 and 2 (MaSp1, MaSp2). These proteins consist of a large central domain composed of approximately 100 tandem copies of a 35-40 amino acid repeat sequence. Non-repetitive N and C-terminal domains, of which the C-terminal domain has been implicated to transition from soluble and insoluble states during spinning, flank the repetitive core. The N-terminal domain until recently has been largely unknown due to difficulties in cloning and expression. Here, we report nearly complete assignment for all (1)H, (13)C, and (15)N resonances in the 14 kDa N-terminal domain of major ampullate spidroin 1 (MaSp1-N) of the golden orb-web spider Nephila clavipes.
authors.affiliation: Department of Biochemistry and Molecular Biology, Medical University of South Carolina, 173 Ashley Ave., BSB 535D, PO Box 250509, Charleston, SC 29425, USA.
authors.forename: Stuart
authors.initials: S
authors.lastname: Parnham
authors.forename: William A
authors.initials: WA
authors.lastname: Gaines
authors.forename: Brendan M
authors.initials: BM
authors.lastname: Duggan
authors.forename: William R
authors.initials: WR
authors.lastname: Marcotte
authors.forename: Mirko
authors.initials: M
authors.lastname: Hennig
mesh_terms: D000818:Animals; D002247:Carbon Isotopes; D005349:Fibroins / Q000737:chemistry*; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D013112:Spiders
chemical_list: D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; C086087:spidroin 1; D005349:Fibroins