Structure of characteristic sequences in Nephila clavipes dragline silk (MaSp1) studied with 13C solid state NMR

The structure of the characteristic sequences in Nephila clavipes dragline silk (MaSp1) were studied using the 13C solid state NMR technique. All the 13C NMR peaks were found to show random coil chemical shifts. Both 13C chemical shifts of the peptide 1 (YGGLGSQGAGRG) in the aqueous solution and in the solid state were same except for the peak broadening of the solid-state NMR spectrum., which indicated that the structure of the peptide 1 in the aqueous solution and in the solid state is random coil. The Ala Cα and Cβ, and Gly Cα chemical shifts of another peptide after AN treatment were same as those of the dragline silk fiber of Nephila clavipes.