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- Cheng, X., et al.
(författare)
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European activities on crosscutting thermal-hydraulic phenomena for innovative nuclear systems
- 2015
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Ingår i: Nuclear Engineering and Design. - : Elsevier BV. - 0029-5493 .- 1872-759X. ; 290, s. 2-12
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Tidskriftsartikel (refereegranskat)abstract
- Thermal-hydraulics is recognized as a key scientific subject in the development of innovative reactor systems. In Europe, a consortium is established consisting of 24 institutions of universities, research centers and nuclear industries with the main objectives to identify and to perform research activities on important crosscutting thermal-hydraulic issues encountered in various innovative nuclear systems. For this purpose the large-scale integrated research project THINS (Thermal-Hydraulics of Innovative Nuclear Systems) is launched in the 7th Framework Programme FP7 of European Union. The main topics considered in the THINS project are (a) advanced reactor core thermal-hydraulics, (b) single phase mixed convection, (c) single phase turbulence, (d) multiphase flow, and (e) numerical code coupling and qualification. The main objectives of the project are: Generation of a data base for the development and validation of new models and codes describing the selected crosscutting thermal-hydraulic phenomena. Development of new physical models and modeling approaches for more accurate description of the crosscutting thermal-hydraulic phenomena. Improvement of the numerical engineering tools for the design analysis of the innovative nuclear systems. This paper describes the technical tasks and methodologies applied to achieve the objectives. Main results achieved so far are summarized. This paper serves also as a guidance of this special issue.
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- Palczewska, M, et al.
(författare)
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Characterization of calretinin I-II as an EF-hand, Ca2+, H+-sensing domain
- 2005
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Ingår i: Protein Science. - : Wiley. - 1469-896X .- 0961-8368. ; 14:7, s. 1879-1887
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Tidskriftsartikel (refereegranskat)abstract
- Calretinin, a neuronal protein with well-defined calcium-binding properties, has a poorly defined function. The pH dependent properties of calretinin (CR), the N-terminal (CR I-II), and C-terminal (CR III-VI) domains were investigated. A drop in pH within the intracellular range (from pH 7.5 to pH 6.5) leads to an increased hydrophobicity of calcium-bound CR and its domains as reported by fluorescence spectroscopy with the hydrophobic probe 2-(p-toluidino)-6-naphthalenesulfonic acid (TNS). The TNS data for the N- and C-terminal domains of CR are additive, providing further support for their independence within the full-length protein. Our work concentrated on CR I-II, which was found to have hydrophobic properties similar to calmodulin at lower pH. The elution of CR I-II from a phenyl-Sepharose column was consistent with the TNS data. The pH-dependent structural changes were further localized to residues 13-28 and 44-51 using nuclear magnetic resonance spectroscopy chemical shift analysis, and there appear to be no large changes in secondary structure. Protonation of His12 and/or His27 side chains, coupled with calcium chelation, appears to lead to the organization of a hydrophobic pocket in the N-terminal domain. CR may sense and respond to calcium, proton, and other signals, contributing to conflicting data on the proteins role as a calcium sensor or calcium buffer.
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- Szabo, Zoltan, Associate professor, et al.
(författare)
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1H and 13C NMR study of novel fused 1,2,4‐triazole heterocycles
- 1992
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Ingår i: Magnetic Resonance in Chemistry. - : Wiley. - 0749-1581 .- 1097-458X. ; 30:11, s. 1111-1116
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Tidskriftsartikel (refereegranskat)abstract
- The 1H and 13C NMR spectra of some novel 1,2,4‐triazolo [1,3] thiazinoquinoline isomeric pairs are interpreted in terms of structural assignments. The structure of most compounds has been confirmed by NOE difference spectroscopy. Characteristic differences have been observed in both 1H and 13C NMR spectra of these isomeric Pairs: some of the 1H and 13C chemical shifts, and also the one bond 13C1H couplings of triazole protons, differ consistently in the NMR spectra of the isomers. The coupling constants have been determined using a combination of INEPT and chemical shift selective filtering.
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