Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/38793
Title: STRUCTURES OF REPETITIVE AND C-TERMINAL DOMAINS OF AN ACINIFORM SPIDROIN AND THEIR ROLES IN SILK FORMATION
Authors: WANG SHUJING
Keywords: spider, silk protein, protein structure, CTD, RP, silk formation
Issue Date: 24-Aug-2012
Source: WANG SHUJING (2012-08-24). STRUCTURES OF REPETITIVE AND C-TERMINAL DOMAINS OF AN ACINIFORM SPIDROIN AND THEIR ROLES IN SILK FORMATION. ScholarBank@NUS Repository.
Abstract: Aciniform spidroin (AcSp1) is so far the only molecular component known to form the Aciniform spider silk, which is tougher than all the other silks and most artificial materials. In order to reveal the mechanism behind the aciniform silk formation and its excellent mechanical properties, we here investigate the solution structure of different domains of AcSp1 and their functional roles in silk formation. In this study, sequences of C-terminal domain (CTD) and repetitive (RP) domains of AcSp1 were identified from a cDNA library and Gdna template. Both CTD and RP were cloned and expressed in an E.coli expression system. The CTD formed oligomers, while a CTD mutant with two amino acid mutations was dimer in aqueous solution. The RP domain was monomer and highly soluble in aqueous solution. Solution structure of the mutant CTD and RP was determined using multi-dimensional NMR techniques. Constructs of multiple (1-4) RP domains with or without CTD were successfully built and expressed in E.coli system. All the purified proteins could quickly form silk fibers under shearing force as long as one RPtr is present in the construct. The number of RP domains does not affect the ability of silk fiber formation but influences the properties of the formed silk fibers.
URI: http://scholarbank.nus.edu.sg/handle/10635/38793
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