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Electrochromic Device Composed of a Di-Urethanesil Electrolyte Incorporating Lithium Triflate and 1-Butyl-3-Methylimidazolium Chloride
Publication . Gonçalves, Maria Cristina; Pereira, Rui F. P.; Alves, Raquel; Nunes, Sílvia C.; Fernandes, Mariana; Gonçalves, Helena M. R.; Pereira, Sónia; Silva, M. Manuela; Fortunato, Elvira; Rego, Rosa; de Zea Bermudez, Verónica; DCM - Departamento de Ciência dos Materiais; Frontiers
A di-urethane cross-linked poly(oxyethylene)/silica hybrid matrix [di-urethanesil, d-Ut(600)], synthesized by the sol-gel process, was doped with lithium triflate (LiCF3SO3) and the 1-butyl-3-methylimidazolium chloride ([Bmim]Cl) ionic liquid. The as-produced xerogel film is amorphous, transparent, flexible, homogeneous, hydrophilic, and has low nanoscale surface roughness. It exhibits an ionic conductivity of 3.64 × 10–6 and 5.00 × 10–4 S cm–1 at 21 and 100°C, respectively. This material was successfully tested as electrolyte in an electrochromic device (ECD) with the glass/ITO/a-WO3/d-Ut(600)10LiCF3SO3[Bmim]Cl/c-NiO/ITO/glass configuration, where a-WO3 and c-NiO stand for amorphous tungsten oxide and crystalline nickel oxide, respectively. The device demonstrated attractive electro-optical performance: fast response times (1–2 s for coloring and 50 s for bleaching), good optical memory [loss of transmittance (T) of only 41% after 3 months, at 555 nm], four mode modulation [bright mode (+3.0 V, T = 77% at 555 nm), semi-bright mode (−1.0 V, T = 60% at 555 nm), dark mode (−1.5 V, T = 38 % at 555 nm), and very dark mode (−2.0 V, T = 11% and −2.5 V, T = 7% at 555 nm)], excellent cycling stability denoting improvement with time, and high coloration efficiency [CEin = −6727 cm2 C–1 (32th cycle) and CEout = +2794 cm2 C–1 (480th cycle), at 555 nm].
Smoothing membrane protein structure determination by initial upstream stage improvements
Publication . Pedro, Augusto Quaresma; Queiroz, João António; Passarinha, Luís António; UCIBIO - Applied Molecular Biosciences Unit; DQ - Departamento de Química; Springer
Membrane proteins (MP) constitute 20–30% of all proteins encoded by the genome of various organisms and perform a wide range of essential biological functions. However, despite they represent the largest class of protein drug targets, a relatively small number high-resolution 3D structures have been obtained yet. Membrane protein biogenesis is more complex than that of the soluble proteins and its recombinant biosynthesis has been a major drawback, thus delaying their further structural characterization. Indeed, the major limitation in structure determination of MP is the low yield achieved in recombinant expression, usually coupled to low functionality, pinpointing the optimization target in recombinant MP research. Recently, the growing attention that have been dedicated to the upstream stage of MP bioprocesses allowed great advances, permitting the evolution of the number of MP solved structures. In this review, we analyse and discuss effective solutions and technical advances at the level of the upstream stage using prokaryotic and eukaryotic organisms foreseeing an increase in expression yields of correctly folded MP and that may facilitate the determination of their three-dimensional structure. A section on techniques used to protein quality control and further structure determination of MP is also included. Lastly, a critical assessment of major factors contributing for a good decision-making process related to the upstream stage of MP is presented.
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Fundação para a Ciência e a Tecnologia
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5876
Número da atribuição
UID/Multi/00709/2013