Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/48583
Title: STRUCTURAL CHARCTERIZATION OF MINOR AMPULLATE SPIDROIN DOMAINS AND THEIR DISTINT ROLES IN FIBROIN SOLUBILITY AND FIBER FORMATION
Authors: GAO ZHENWEI
Keywords: NMR structure, spider silk protein, minor ampullate spidroin, protein strorage, fiber formation, protein stability
Issue Date: 19-Aug-2013
Source: GAO ZHENWEI (2013-08-19). STRUCTURAL CHARCTERIZATION OF MINOR AMPULLATE SPIDROIN DOMAINS AND THEIR DISTINT ROLES IN FIBROIN SOLUBILITY AND FIBER FORMATION. ScholarBank@NUS Repository.
Abstract: Spider silk is protein fibers with extraordinary mechanical properties. Up to now, it is still poorly understood how silk proteins are kept in a soluble form before spinning into fibers and how the protein molecules are aligned orderly to form fibers. Minor ampullate spidroin is one of the seven types of silk proteins, which consists of four types of domains: N-terminal domain, C-terminal domain (CTD), repetitive domain (RP) and linker domain (LK). Here we report the tertiary structure of CTD and RP and secondary structures of NTD and LK in aqueous solution. Stability, solubility and other biophysical studies on the single domains and different fragments reveal that they all play distinct roles in fiber formation. Finally, a simple model of spider silk protein storage and fiber formation is proposed.
URI: http://scholarbank.nus.edu.sg/handle/10635/48583
Appears in Collections:Ph.D Theses (Open)

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