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13C NMR spectrum of the regenerated sericin solution (Figure 3a) exhibited much smaller peaks assignable to Glu, Phe, and Tyr residues than native sericin solution (Figure la), showing that low molecular weight impurities can be removed during regeneration process. The Cα and Cβ chemical shifts of major amino acids in the regenerated sericin solution were in good agreement with those of native sericin solution, which demonstrated that sericin remained in a largely random coil structure after regeneration from the cocoon.
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