Abstract：
:Silk is spun from the liquid precursor known as liquid silk secreted from the posterior part and stored in the silk gland lumen with occurrence of many momentary events. The liquid silk in the silk gland is transformed to the spun silk fibre. In this study the elucidation of the protein components of liquid silk from the posterior part of the silk gland (PSG) of saturniid silkworm Antheraea assamensis along with its structural characterization has been reported. The 3D model of the N-terminal amorphous portion with some repeat crystalline motifs (19-255) of core protein fibroin has also been constructed. 1D and 2D electrophoresis revealed the homo-dimeric structure of the silk protein. Secondary structure analysis by Circular dichroism, FTIR spectroscopy showed α helical structural component as predominant conformation in the liquid silk. The crystalline structure investigated through X ray diffraction (XRD) analysis also revealed the presence of less ordered amorphous α helical conformation in the liquid silk. The 3D structural model proposed of the residues from 19 to 255 has revealed structural stability throughout the molecular dynamics simulation process. This study will provide the detailed structural information and in silico analysis of the core protein present in the liquid silk of PSG.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Goswami A,Goswami N,Bhattacharya A,Borah P,Devi Ddoi
10.1016/j.ijbiomac.2020.08.232subject
Has Abstractpub_date
2020-11-15 00:00:00pages
1947-1958eissn
0141-8130issn
1879-0003pii
S0141-8130(20)34329-4journal_volume
163pub_type
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