| 1. |
- Hedhammar, My, Professor, 1975-, et al.
(författare)
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Structural properties of recombinant nonrepetitive and repetitive parts of major ampullate spidroin 1 from Euprosthenops australis : implications for fiber formation
- 2008
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Ingår i: Journal of Biotechnology. - : American Chemical Society (ACS). - 0168-1656 .- 1873-4863. ; 47:11, s. 3407-17
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Tidskriftsartikel (refereegranskat)abstract
- Spider dragline silk proteins, spidroins, have a tripartite composition; a nonrepetitive N-terminal domain, a central repetitive region built up from many iterated poly-Ala and Gly rich blocks, and a C-terminal nonrepetitive domain. It is generally believed that the repetitive region forms intermolecular contacts in the silk fibers, while precise functions of the terminal domains have not been established. Herein, thermal, pH, and salt effects on the structure and aggregation and/or polymerization of recombinant N- and C-terminal domains, a repetitive segment containing four poly-Ala and Gly rich coblocks, and combinations thereof were studied. The N- and C-terminal domains have mainly alpha-helical structure, and interestingly, both form homodimers. Dimerization of the end domains allows spidroin multimerization independent of the repetitive part. Reduction of an intersubunit disulfide in the C-terminal domain lowers the thermal stability but does not affect dimerization. The repetitive region shows helical secondary structure but appears to lack stable folded structure. A protein composed of this repetitive region linked to the C-terminal domain has a mainly alpha-helical folded structure but shows an abrupt transition to beta-sheet structures upon heating. At room temperature, this protein self-assembles into macroscopic fibers within minutes. The secondary structures of none of the domains are altered by pH or salt. However, high concentrations of phosphate affect the tertiary structure and accelerate the aggregation propensity of the repetitive region. Implications of these results for dragline spidroin behavior in solution and silk fiber formation are discussed.
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| 2. |
- Liu, Hao, et al.
(författare)
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A thermodynamic study of hot syngas impurities in steel reheating furnaces : Corrosion and interaction with oxide scales
- 2014
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Ingår i: Energy. - : Elsevier BV. - 0360-5442 .- 1873-6785. ; 77, s. 352-361
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Tidskriftsartikel (refereegranskat)abstract
- Environmental concerns lead industries to implement gasified biomass (syngas) as a promising fuel in steel reheating furnaces. The impurities of syngas as well as a combination with iron oxide scale form complex mixtures with low melting points, and might cause corrosion on steel slabs. In this paper, the effects of syngas impurities are thermodynamically investigated, when scale formation on the steel slabs surface simultaneously takes place. A steel reheating furnace can be divided into preheating, heating, and soaking zones where the temperature of a steel slab changes respectively. Therefore, the thermodynamic calculation is performed at different temperatures to predict the fate of impurities. Then, the stable species are connected with respective zones in a reheating furnace. It is concluded that reactions due to alkali compounds, chloride, and particulate matter could take place on steel slabs. In the low temperature range, interaction of sodium chloride occured with pure iron prior to scale formation. Then, at high temperature the reactions of impurities are notable with iron oxides due to scale growing. Furthermore, the multicomponent reactions with syngas impurities showed that most of alkali contents evaporate at first stages, and only small amounts of them remain in slag at high temperature.
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| 3. |
- Stark, M., et al.
(författare)
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Macroscopic fibers self-assembled from recombinant miniature spider silk proteins
- 2007
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Ingår i: Biomacromolecules. - : American Chemical Society (ACS). - 1525-7797 .- 1526-4602. ; 8:5, s. 1695-1701
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Tidskriftsartikel (refereegranskat)abstract
- Strength, elasticity, and biocompatibility make spider silk an attractive resource for the production of artificial biomaterials. Spider silk proteins, spidroins, contain hundreds of repeated poly alanine/glycine-rich blocks and are difficult to produce recombinantly in soluble form. Most previous attempts to produce artificial spider silk fibers have included solubilization steps in nonphysiological solvents. It is here demonstrated that a miniature spidroin from a protein in dragline silk of Euprosthenops australis can be produced in a soluble form in Escherichia coli when fused to a highly soluble protein partner. Although this miniature spidroin contains only four poly alanine/glycine-rich blocks followed by a C-terminal non-repetitive domain, meter-long fibers are spontaneously formed after proteolytic release of the fusion partner. The structure of the fibers is similar to that of dragline silks, and although self-assembled from recombinant proteins they are as strong as fibers spun from redissolved silk. Moreover, the fibers appear to be biocompatible because human tissue culture cells can grow on and attach to the fibers. These findings enable controlled production of high-performance biofibers at large scale under physiological conditions.
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