Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0056142
Title: Structural Characterization of Minor Ampullate Spidroin Domains and Their Distinct Roles in Fibroin Solubility and Fiber Formation
Authors: Gao, Z.
Lin, Z. 
Huang, W. 
Lai, C.C.
Fan, J.-S. 
Yang, D. 
Issue Date: 13-Feb-2013
Citation: Gao, Z., Lin, Z., Huang, W., Lai, C.C., Fan, J.-S., Yang, D. (2013-02-13). Structural Characterization of Minor Ampullate Spidroin Domains and Their Distinct Roles in Fibroin Solubility and Fiber Formation. PLoS ONE 8 (2) : -. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0056142
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 secondary structures of RP and LK in aqueous solution, and their roles in protein stability, solubility and fiber formation. The stability and solubility of individual domains are dramatically different and can be explained by their distinct structures. For the tri-domain miniature fibroin, RP-LK-CTDMi, the three domains have no or weak interactions with one another at low protein concentrations (
Source Title: PLoS ONE
URI: http://scholarbank.nus.edu.sg/handle/10635/101758
ISSN: 19326203
DOI: 10.1371/journal.pone.0056142
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