The four proteins were designated as S. marmorata silk proteins (Smsps)-1�4.  The molecular mass of Smsp-1 is mostly as large as that of Bombyx mori Fibroin H.  The present study describes the amino acid analysis and partial sequences of Smsp-1.  The content of Gly is the highest level at 24%, and those of Ala, Ser, Tyr, Glx (Glu+Gln), Pro, and Val are ranging from 7 to 9%.  The composition of Smsp-1 is characteristic for less Ala and higher Pro contents, as compared with that of Fibroin H.  N-terminal sequencing of Smsp-1 reveals a repeating motif composed of Pro, Tyr, Gly, and Asp, and the similar sequences were found in 7 kinds of tryptic fragments from the crude silk gland protein preparation containing Smsp-1�4, suggesting that the Smsp-1 has molecular characteristics different from the Fibroin H.

Repetitive sequential motifs of underwater silk protein from caddisfly, <i>Stenopsyche marmorata</i>

243rd National Meeting (2012)

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Repetitive sequential motifs of underwater silk protein from caddisfly, Stenopsyche marmorata