Structural Characterization of Minor Ampullate Spidroin Domains and Their Distinct Roles in Fibroin Solubility and Fiber Formation
| Autor: | Jing-Song Fan, Daiwen Yang, Weidong Huang, Zhi Lin, Chong Cheong Lai, Zhenwei Gao |
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| Jazyk: | angličtina |
| Rok vydání: | 2013 |
| Předmět: |
Models
Molecular Protein Denaturation Low protein Polymers lcsh:Medicine Protein aggregation Biochemistry Protein Structure Secondary Protein structure Biopolymers Materials Chemistry Spider silk lcsh:Science Multidisciplinary Spidroin Chemistry Protein Stability Circular Dichroism Temperature Spiders Materials Characterization Material by Structure Research Article Protein Structure Protein domain Materials Science Material Properties Molecular Sequence Data Silk Fibroin Biomaterials Sequence Homology Nucleic Acid Mechanical Properties Animals Amino Acid Sequence Protein Interactions Biology Protein Unfolding Binding Sites Base Sequence Sequence Homology Amino Acid lcsh:R fungi Proteins Protein tertiary structure Protein Structure Tertiary Solubility Mutation Biophysics Microscopy Electron Scanning lcsh:Q Fibroins |
| Zdroj: | PLoS ONE PLoS ONE, Vol 8, Iss 2, p e56142 (2013) |
| ISSN: | 1932-6203 |
| Popis: | 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-CTD(Mi), the three domains have no or weak interactions with one another at low protein concentrations ( |
| Databáze: | OpenAIRE |
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