NMR assignments of the N-terminal domain of Nephila clavipes spidroin 1

作者：Parnham Stuart; Gaines William A; Duggan Brendan M; Marcotte William R Jr; Hennig Mirko^*

来源：Biomolecular NMR Assignments, 2011, 5(2): 131-133.

DOI：10.1007/s12104-010-9284-z

• Spider dragline silk
• Major ampullate spidroin
• N-terminal domain
• Nephila clavipes

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.

• 出版日期2011-10