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  • 1
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    New Directions on Model Predictive Control (2021)
    MDPI - Multidisciplinary Digital Publishing Institute
    Details
    Publication Date: 2024-04-11
    Description: Model predictive control (MPC) is an advanced control design used in many industries worldwide. An MPC selects control actions which are optimal with respect to a given performance metric as well as any physically-motivated constraints. MPC has therefore gained significant research attention over the past several decades. Advances in MPC continue to unlock its potential to solve a wide variety of practical issues. This book presents some of the state-of-the-art in MPC design from theoretical and applications perspectives. It covers a broad spectrum of MPC application areas, reviewing applications as diverse as air conditioning, pharmaceutical manufacturing, mineral column flotation, actuator faults, and hydraulic fracturing, while also highlighting recent theoretical advancements in control technology that integrate it with data-driven models, zone tracking, or process safety and cybersecurity. Both centralized and distributed MPC formulations are presented. The purpose of this book is to assemble a collection of current research in MPC that handles practically-motivated theoretical issues as well as recent MPC applications, with the aim of highlighting the significant potential benefits of new MPC theory and design.
    Keywords: TA1-2040 ; receding horizon control ; optimal control ; predictive control ; thema EDItEUR::T Technology, Engineering, Agriculture, Industrial processes::TB Technology: general issues::TBX History of engineering and technology
    Language: English
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  • 2
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    Structural insight into the mechanism of stabilization of the 7SK small nuclear RNA by LARP7 (2015)
    Oxford University Press
    Details
    Publication Date: 2015-04-02
    Description: The non-coding RNA 7SK is the scaffold for a small nuclear ribonucleoprotein (7SKsnRNP) which regulates the function of the positive transcription elongation factor P-TEFb in the control of RNA polymerase II elongation in metazoans. The La-related protein LARP7 is a component of the 7SKsnRNP required for stability and function of the RNA. To address the function of LARP7 we determined the crystal structure of its La module, which binds a stretch of uridines at the 3'-end of 7SK. The structure shows that the penultimate uridine is tethered by the two domains, the La-motif and the RNA-recognition motif (RRM1), and reveals that the RRM1 is significantly smaller and more exposed than in the La protein. Sequence analysis suggests that this impacts interaction with 7SK. Binding assays, footprinting and small-angle scattering experiments show that a second RRM domain located at the C-terminus binds the apical loop of the 3' hairpin of 7SK, while the N-terminal domains bind at its foot. Our results suggest that LARP7 uses both its N- and C-terminal domains to stabilize 7SK in a closed structure, which forms by joining conserved sequences at the 5'-end with the foot of the 3' hairpin and has thus functional implications.
    Print ISSN: 0305-1048
    Electronic ISSN: 1362-4962
    Topics: Biology
    Published by Oxford University Press
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  • 3
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    Dominance hierarchy arising from the evolution of a complex small RNA regulatory network (2014)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2014-12-06
    Description: The prevention of fertilization through self-pollination (or pollination by a close relative) in the Brassicaceae plant family is determined by the genotype of the plant at the self-incompatibility locus (S locus). The many alleles at this locus exhibit a dominance hierarchy that determines which of the two allelic specificities of a heterozygous genotype is expressed at the phenotypic level. Here, we uncover the evolution of how at least 17 small RNA (sRNA)-producing loci and their multiple target sites collectively control the dominance hierarchy among alleles within the gene controlling the pollen S-locus phenotype in a self-incompatible Arabidopsis species. Selection has created a dynamic repertoire of sRNA-target interactions by jointly acting on sRNA genes and their target sites, which has resulted in a complex system of regulation among alleles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Durand, Eleonore -- Meheust, Raphael -- Soucaze, Marion -- Goubet, Pauline M -- Gallina, Sophie -- Poux, Celine -- Fobis-Loisy, Isabelle -- Guillon, Eline -- Gaude, Thierry -- Sarazin, Alexis -- Figeac, Martin -- Prat, Elisa -- Marande, William -- Berges, Helene -- Vekemans, Xavier -- Billiard, Sylvain -- Castric, Vincent -- New York, N.Y. -- Science. 2014 Dec 5;346(6214):1200-5. doi: 10.1126/science.1259442.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire Genetique et Evolution des Populations Vegetales, CNRS UMR 8198, Universite Lille 1, F-59655 Villeneuve d'Ascq cedex, France. ; Reproduction et Developpement des Plantes, Institut Federatif de Recherche 128, Centre National de la Recherche Scientifique, Institut National de la Recherche Agronomique, Universite Claude Bernard Lyon I, Ecole Normale Superieure de Lyon, F-69364 Lyon, Cedex 07, France. ; Department of Biology, Swiss Federal Institute of Technology Zurich, CH-8093 Zurich, Switzerland. ; UDSL Universite Lille 2 Droit et Sante, and Plate-forme de genomique fonctionnelle et structurale IFR-114, F-59000 Lille, France. ; Centre National des Ressources Genomiques Vegetales, INRA UPR 1258, Castanet-Tolosan, France. ; Laboratoire Genetique et Evolution des Populations Vegetales, CNRS UMR 8198, Universite Lille 1, F-59655 Villeneuve d'Ascq cedex, France. vincent.castric@univ-lille1.fr.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25477454" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Arabidopsis/*genetics ; *Biological Evolution ; *Gene Expression Regulation, Plant ; *Gene Regulatory Networks ; *Genes, Dominant ; *Genes, Recessive ; Genetic Loci ; Models, Molecular ; Phylogeny ; Pollination ; RNA, Small Untranslated/classification/*genetics ; Selection, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    Molecular trade-offs in RNA ligases affected the modular emergence of complex ribozymes at the origin of life (2017)
    Royal Society
    Details
    Publication Date: 2017-09-21
    Description: In the RNA world hypothesis complex, self-replicating ribozymes were essential. For the emergence of an RNA world, less is known about the early processes that accounted for the formation of complex, long catalysts from small passively formed molecules. The functional role of small sequences has not been fully explored and, here, a possible role for smaller ligases is demonstrated. An established RNA polymerase model, the R18, was truncated from the 3' end to generate smaller molecules. All the molecules were investigated for self-ligation functions with a set of oligonucleotide substrates without predesigned base pairing. The smallest molecule that exhibited self-ligation activity was a 40-nucleotide RNA. It also demonstrated the greatest functional flexibility as it was more general in the kinds of substrates it ligated to itself although its catalytic efficiency was the lowest. The largest ribozyme (R18) ligated substrates more selectively and with greatest efficiency. With increase in size and predicted structural stability, self-ligation efficiency improved, while functional flexibility decreased. These findings reveal that molecular size could have increased from the activity of small ligases joining oligonucleotides to their own end. In addition, there is a size-associated molecular-level trade-off that could have impacted the evolution of RNA-based life.
    Keywords: molecular biology, evolution, astrobiology
    Electronic ISSN: 2054-5703
    Topics: Natural Sciences in General
    Published by Royal Society
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  • 5
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    Priming and polymerization of a bacterial contractile tail structure (2016)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2016-02-26
    Description: Contractile tails are composed of an inner tube wrapped by an outer sheath assembled in an extended, metastable conformation that stores mechanical energy necessary for its contraction. Contraction is used to propel the rigid inner tube towards target cells for DNA or toxin delivery. Although recent studies have revealed the structure of the contractile sheath of the type VI secretion system, the mechanisms by which its polymerization is controlled and coordinated with the assembly of the inner tube remain unknown. Here we show that the starfish-like TssA dodecameric complex interacts with tube and sheath components. Fluorescence microscopy experiments in enteroaggregative Escherichia coli reveal that TssA binds first to the type VI secretion system membrane core complex and then initiates tail polymerization. TssA remains at the tip of the growing structure and incorporates new tube and sheath blocks. On the basis of these results, we propose that TssA primes and coordinates tail tube and sheath biogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zoued, Abdelrahim -- Durand, Eric -- Brunet, Yannick R -- Spinelli, Silvia -- Douzi, Badreddine -- Guzzo, Mathilde -- Flaugnatti, Nicolas -- Legrand, Pierre -- Journet, Laure -- Fronzes, Remi -- Mignot, Tam -- Cambillau, Christian -- Cascales, Eric -- England -- Nature. 2016 Mar 3;531(7592):59-63. doi: 10.1038/nature17182. Epub 2016 Feb 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire d'Ingenierie des Systemes Macromoleculaires, Institut de Microbiologie de la Mediterranee, CNRS UMR7255, Aix-Marseille Universite, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France. ; Architecture et Fonction des Macromolecules Biologiques, Centre National de la Recherche Scientifique, UMR 7257, Campus de Luminy, Case 932, 13288 Marseille Cedex 09, France. ; Architecture et Fonction des Macromolecules Biologiques, Aix-Marseille Universite, UMR 7257, Campus de Luminy, Case 932, 13288 Marseille Cedex 09, France. ; G5 Biologie structurale de la secretion bacterienne, Institut Pasteur, 25-28 rue du Docteur Roux, 75015 Paris, France. ; UMR 3528, CNRS, Institut Pasteur, 25-28 rue du Docteur Roux, 75015 Paris, France. ; Laboratoire de Chimie Bacterienne, Institut de Microbiologie de la Mediterranee, CNRS UMR7283, Aix-Marseille Universite, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France. ; Synchrotron Soleil, L'Orme des merisiers, Saint-Aubin BP48, 91192 Gif-sur-Yvette Cedex, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26909579" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallography, X-Ray ; Escherichia coli/*chemistry/ultrastructure ; Escherichia coli Proteins/*chemistry/*metabolism/ultrastructure ; Microscopy, Electron ; Microscopy, Fluorescence ; Models, Molecular ; *Polymerization ; Protein Structure, Tertiary ; Type VI Secretion Systems/chemistry/metabolism/ultrastructure
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 6
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    Biogenesis and structure of a type VI secretion membrane core complex (2015)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2015-07-23
    Description: Bacteria share their ecological niches with other microbes. The bacterial type VI secretion system is one of the key players in microbial competition, as well as being an important virulence determinant during bacterial infections. It assembles a nano-crossbow-like structure in the cytoplasm of the attacker cell that propels an arrow made of a haemolysin co-regulated protein (Hcp) tube and a valine-glycine repeat protein G (VgrG) spike and punctures the prey's cell wall. The nano-crossbow is stably anchored to the cell envelope of the attacker by a membrane core complex. Here we show that this complex is assembled by the sequential addition of three type VI subunits (Tss)-TssJ, TssM and TssL-and present a structure of the fully assembled complex at 11.6 A resolution, determined by negative-stain electron microscopy. With overall C5 symmetry, this 1.7-megadalton complex comprises a large base in the cytoplasm. It extends in the periplasm via ten arches to form a double-ring structure containing the carboxy-terminal domain of TssM (TssMct) and TssJ that is anchored in the outer membrane. The crystal structure of the TssMct-TssJ complex coupled to whole-cell accessibility studies suggest that large conformational changes induce transient pore formation in the outer membrane, allowing passage of the attacking Hcp tube/VgrG spike.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Durand, Eric -- Nguyen, Van Son -- Zoued, Abdelrahim -- Logger, Laureen -- Pehau-Arnaudet, Gerard -- Aschtgen, Marie-Stephanie -- Spinelli, Silvia -- Desmyter, Aline -- Bardiaux, Benjamin -- Dujeancourt, Annick -- Roussel, Alain -- Cambillau, Christian -- Cascales, Eric -- Fronzes, Remi -- England -- Nature. 2015 Jul 30;523(7562):555-60. doi: 10.1038/nature14667. Epub 2015 Jul 22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] Laboratoire d'Ingenierie des Systemes Macromoleculaires, Aix-Marseille Universite - CNRS, UMR 7255, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France [2] Architecture et Fonction des Macromolecules Biologiques, CNRS, UMR 7257, Campus de Luminy, Case 932, 13288 Marseille Cedex 09, France [3] G5 Biologie structurale de la secretion bacterienne, Institut Pasteur, 25-28 rue du Docteur Roux, 75015 Paris, France [4] UMR 3528, CNRS, Institut Pasteur, 25-28 rue du Docteur Roux, 75015 Paris, France [5] AFMB, Aix-Marseille Universite, IHU Mediterranee Infection, Campus de Luminy, Case 932, 13288 Marseille Cedex 09, France. ; 1] Architecture et Fonction des Macromolecules Biologiques, CNRS, UMR 7257, Campus de Luminy, Case 932, 13288 Marseille Cedex 09, France [2] AFMB, Aix-Marseille Universite, IHU Mediterranee Infection, Campus de Luminy, Case 932, 13288 Marseille Cedex 09, France. ; Laboratoire d'Ingenierie des Systemes Macromoleculaires, Aix-Marseille Universite - CNRS, UMR 7255, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France. ; UMR 3528, CNRS, Institut Pasteur, 25-28 rue du Docteur Roux, 75015 Paris, France. ; 1] UMR 3528, CNRS, Institut Pasteur, 25-28 rue du Docteur Roux, 75015 Paris, France [2] Unite de Bioinformatique Structurale, Institut Pasteur, 25-28 rue du Docteur Roux, 75015 Paris, France. ; 1] G5 Biologie structurale de la secretion bacterienne, Institut Pasteur, 25-28 rue du Docteur Roux, 75015 Paris, France [2] UMR 3528, CNRS, Institut Pasteur, 25-28 rue du Docteur Roux, 75015 Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26200339" target="_blank"〉PubMed〈/a〉
    Keywords: *Bacterial Secretion Systems ; Cell Membrane/chemistry/metabolism ; Crystallography, X-Ray ; Cytoplasm/chemistry/metabolism ; Escherichia coli/*chemistry/metabolism ; Escherichia coli Proteins/biosynthesis/*chemistry ; Lipopeptides/biosynthesis/*chemistry ; Membrane Proteins/biosynthesis/*chemistry ; Microscopy, Electron ; Models, Molecular ; Multiprotein Complexes/*biosynthesis/*chemistry ; Periplasm/chemistry/metabolism ; Porosity ; Protein Structure, Tertiary ; Protein Subunits/biosynthesis/chemistry
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 7
    Electronic Resource
    Electronic Resource
    Split model description of the copper site distribution in the new layered (2D) copper vanadium phosphorus sulfide (CuIVIIIP2S6) phase (1990)
    s.l. : American Chemical Society
    Inorganic chemistry 29 (1990), S. 4916-4920 
    Details
    ISSN: 1520-510X
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ic00349a019
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  • 8
    Electronic Resource
    Electronic Resource
    The Melting of Binary Eutectics1 (1952)
    s.l. : American Chemical Society
    Journal of the American Chemical Society 74 (1952), S. 1071-1073 
    Details
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ja01124a064
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  • 9
    Electronic Resource
    Electronic Resource
    Interfacial and Surface Characterization of Fluorine Treated SnAgCu and NiTi Powders and NiTi/SnAgCu Composite Materials (2007)
    s.l. ; Stafa-Zurich, Switzerland
    Materials science forum Vol. 534-536 (Jan. 2007), p. 1461-1464 
    Details
    ISSN: 1662-9752
    Source: Scientific.Net: Materials Science & Technology / Trans Tech Publications Archiv 1984-2008
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: NiTi shape memory alloy particles have been incorporated inside SnAgCu lead freesolder paste in order to improve the mechanical performances of solder paste. However, because ofthe non-wetting properties of solid NiTi particles by the liquid SnAgCu matrix, the development offluorine gas treatment of both NiTi and SnAgCu particles has been optimized. Scanning electronmicroscopy (SEM) micrographs of NiTi/SnAgCu composite materials have shown that “Fluorinetreatment” of SnAgCu powders lead to a huge increase of the NiTi powder content inside theliquid SnAgCu matrix where no effect have been observed when NiTi materials are fluorinated. Xrayphotoelectron spectroscopy analysis of treated SnAgCu powders have been used in order toanalyze surface chemistry evolution where wavelength dispersion spectroscopy line profiles, acrossNiTi-SnAgCu interfaces, have been performed
    Type of Medium: Electronic Resource
    URL: http://www.tib-hannover.de/fulltexts/2011/0528/02/14/transtech_doi~10.4028%252Fwww.scientific.net%252FMSF.534-536.1461.pdf
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  • 10
    Electronic Resource
    Electronic Resource
    Exceptional Performance of a Nuclear Ignition Otto-cycle Engine using n -Pentane as Fuel (1950)
    [s.l.] : Nature Publishing Group
    Nature 166 (1950), S. 70-71 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The usual temperature conditions of engine operation, especially those of the C.F.R.-A.S.T.M. knock-rating procedure, are such that finely divided carbon is obtained after spark ignition by method (a). It is possible, however, to provide low surface-temperature conditions in which the carbon is ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/166070b0
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