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  • 1
    Publication Date: 2011-03-03
    Description: The design and construction of a prototype of a dividing-wall distillation column was possible by integrating previous knowledge in process intensification, energy savings, theoretical control properties, and closed-loop dynamics of thermally coupled distillation sequences. In order to achieve the predicted energy savings for this class of complex distillation column, a dividing wall and a side tank were implemented in order to manipulate the internal flows associated with energy consumption. The reaction between ethanol and acetic acid was conducted within the prototype, and the experimental results indicate that a heterogeneous mixture of ethyl acetate and water is obtained as the top product. The temperature profile measured during the experimental run can be used for controlling the batch distillation column in cyclic operation mode. Reactive distillation is considered the most representative case of process intensification. In this context, a dividing-wall distillation column was designed, implemented and instrumented in order to carry out the production of ethyl acetate. The result indicates that it is possible to obtain an azeotrope of ethyl acetate-water as top product.
    Print ISSN: 0930-7516
    Electronic ISSN: 1521-4125
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Published by Wiley
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  • 2
    Publication Date: 2013-06-12
    Description: Author(s): Y. Bonder, E. Fischbach, H. Hernandez-Coronado, D. E. Krause, Z. Rohrbach, and D. Sudarsky We develop a framework to test the equivalence principle under conditions where the quantum aspects of nature cannot be neglected, specifically in the context of interference phenomena with unstable particles. We derive the nonrelativistic quantum equation that describes the evolution of the wave fu... [Phys. Rev. D 87, 125021] Published Tue Jun 11, 2013
    Keywords: Field theory, formal particle theory
    Print ISSN: 0556-2821
    Electronic ISSN: 1089-4918
    Topics: Physics
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  • 3
    Publication Date: 2013-09-22
    Description: Energy & Fuels DOI: 10.1021/ef401150w
    Print ISSN: 0887-0624
    Electronic ISSN: 1520-5029
    Topics: Chemistry and Pharmacology , Energy, Environment Protection, Nuclear Power Engineering , Process Engineering, Biotechnology, Nutrition Technology
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  • 4
    Publication Date: 2013-03-01
    Electronic ISSN: 2158-3226
    Topics: Physics
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  • 5
    Publication Date: 2012-06-21
    Description: Author(s): H. Hernandez-Coronado, M. Coronado, and E. C. Herrera-Hernandez In this paper an advective-dispersion equation with scale-dependent coefficients is proposed for describing transport through fractals. This equation is obtained by imposing scale invariance and assuming that the porosity, the dispersion coefficient, and the velocity follow fractional power laws on ... [Phys. Rev. E 85, 066316] Published Wed Jun 20, 2012
    Keywords: Fluid dynamics
    Print ISSN: 1539-3755
    Electronic ISSN: 1550-2376
    Topics: Physics
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  • 6
    Publication Date: 2011-08-11
    Description: Author(s): Martin Bojowald, David Brizuela, Hector H. Hernández, Michael J. Koop, and Hugo A. Morales-Técotl When quantum back-reaction by fluctuations, correlations and higher moments of a state becomes strong, semiclassical quantum mechanics resembles a dynamical system with a high-dimensional phase space. Here, systematic computational methods to derive the dynamical equations including all quantum corr... [Phys. Rev. D 84, 043514] Published Wed Aug 10, 2011
    Keywords: Astrophysics & Cosmology
    Print ISSN: 0556-2821
    Electronic ISSN: 1089-4918
    Topics: Physics
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  • 7
    Publication Date: 2014-09-16
    Description: The Journal of Physical Chemistry B DOI: 10.1021/jp506592k
    Electronic ISSN: 1520-5207
    Topics: Chemistry and Pharmacology , Physics
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  • 8
    Publication Date: 2010-04-07
    Description: Targeting of proteins to appropriate subcellular compartments is a crucial process in all living cells. Secretory and membrane proteins usually contain an amino-terminal signal peptide, which is recognized by the signal recognition particle (SRP) when nascent polypeptide chains emerge from the ribosome. The SRP-ribosome nascent chain complex is then targeted through its GTP-dependent interaction with SRP receptor to the protein-conducting channel on endoplasmic reticulum membrane in eukaryotes or plasma membrane in bacteria. A universally conserved component of SRP (refs 1, 2), SRP54 or its bacterial homologue, fifty-four homologue (Ffh), binds the signal peptides, which have a highly divergent sequence divisible into a positively charged n-region, an h-region commonly containing 8-20 hydrophobic residues and a polar c-region. No structure has been reported that exemplifies SRP54 binding of any signal sequence. Here we have produced a fusion protein between Sulfolobus solfataricus SRP54 (Ffh) and a signal peptide connected via a flexible linker. This fusion protein oligomerizes in solution through interaction between the SRP54 and signal peptide moieties belonging to different chains, and it is functional, as demonstrated by its ability to bind SRP RNA and SRP receptor FtsY. We present the crystal structure at 3.5 A resolution of an SRP54-signal peptide complex in the dimer, which reveals how a signal sequence is recognized by SRP54.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2897128/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2897128/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Janda, Claudia Y -- Li, Jade -- Oubridge, Chris -- Hernandez, Helena -- Robinson, Carol V -- Nagai, Kiyoshi -- MC_U105184330/Medical Research Council/United Kingdom -- U.1051.04.016(78933)/Medical Research Council/United Kingdom -- Medical Research Council/United Kingdom -- England -- Nature. 2010 May 27;465(7297):507-10. doi: 10.1038/nature08870. Epub 2010 Apr 4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20364120" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/metabolism ; Crystallography, X-Ray ; Mass Spectrometry ; Models, Molecular ; Molecular Sequence Data ; Protein Binding ; Protein Multimerization ; Protein Sorting Signals/*physiology ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Receptors, Cytoplasmic and Nuclear/metabolism ; Receptors, Virus/metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Signal Recognition Particle/*chemistry/*metabolism ; Structure-Activity Relationship ; Sulfolobus solfataricus/*chemistry
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 9
    Publication Date: 2011-12-23
    Description: Human immunodeficiency virus (HIV) has a small genome and therefore relies heavily on the host cellular machinery to replicate. Identifying which host proteins and complexes come into physical contact with the viral proteins is crucial for a comprehensive understanding of how HIV rewires the host's cellular machinery during the course of infection. Here we report the use of affinity tagging and purification mass spectrometry to determine systematically the physical interactions of all 18 HIV-1 proteins and polyproteins with host proteins in two different human cell lines (HEK293 and Jurkat). Using a quantitative scoring system that we call MiST, we identified with high confidence 497 HIV-human protein-protein interactions involving 435 individual human proteins, with approximately 40% of the interactions being identified in both cell types. We found that the host proteins hijacked by HIV, especially those found interacting in both cell types, are highly conserved across primates. We uncovered a number of host complexes targeted by viral proteins, including the finding that HIV protease cleaves eIF3d, a subunit of eukaryotic translation initiation factor 3. This host protein is one of eleven identified in this analysis that act to inhibit HIV replication. This data set facilitates a more comprehensive and detailed understanding of how the host machinery is manipulated during the course of HIV infection.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3310911/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3310911/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jager, Stefanie -- Cimermancic, Peter -- Gulbahce, Natali -- Johnson, Jeffrey R -- McGovern, Kathryn E -- Clarke, Starlynn C -- Shales, Michael -- Mercenne, Gaelle -- Pache, Lars -- Li, Kathy -- Hernandez, Hilda -- Jang, Gwendolyn M -- Roth, Shoshannah L -- Akiva, Eyal -- Marlett, John -- Stephens, Melanie -- D'Orso, Ivan -- Fernandes, Jason -- Fahey, Marie -- Mahon, Cathal -- O'Donoghue, Anthony J -- Todorovic, Aleksandar -- Morris, John H -- Maltby, David A -- Alber, Tom -- Cagney, Gerard -- Bushman, Frederic D -- Young, John A -- Chanda, Sumit K -- Sundquist, Wesley I -- Kortemme, Tanja -- Hernandez, Ryan D -- Craik, Charles S -- Burlingame, Alma -- Sali, Andrej -- Frankel, Alan D -- Krogan, Nevan J -- P01 AI090935/AI/NIAID NIH HHS/ -- P01 AI090935-02/AI/NIAID NIH HHS/ -- P01 GM073732-05/GM/NIGMS NIH HHS/ -- P41 GM103481/GM/NIGMS NIH HHS/ -- P41 RR001081/RR/NCRR NIH HHS/ -- P41RR001614/RR/NCRR NIH HHS/ -- P50 GM081879/GM/NIGMS NIH HHS/ -- P50 GM081879-02/GM/NIGMS NIH HHS/ -- P50 GM082250/GM/NIGMS NIH HHS/ -- P50 GM082250-05/GM/NIGMS NIH HHS/ -- P50GM081879/GM/NIGMS NIH HHS/ -- P50GM082545/GM/NIGMS NIH HHS/ -- U54 RR022220/RR/NCRR NIH HHS/ -- England -- Nature. 2011 Dec 21;481(7381):365-70. doi: 10.1038/nature10719.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Pharmacology, University of California, San Francisco, California 94158, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22190034" target="_blank"〉PubMed〈/a〉
    Keywords: Affinity Labels ; Amino Acid Sequence ; Conserved Sequence ; Eukaryotic Initiation Factor-3/chemistry/metabolism ; HEK293 Cells ; HIV Infections/metabolism/virology ; HIV Protease/metabolism ; HIV-1/*chemistry/*metabolism/physiology ; *Host-Pathogen Interactions ; Human Immunodeficiency Virus Proteins/analysis/chemistry/isolation & ; purification/*metabolism ; Humans ; Immunoprecipitation ; Jurkat Cells ; Mass Spectrometry ; Protein Binding ; Protein Interaction Mapping/*methods ; Protein Interaction Maps/*physiology ; Reproducibility of Results ; Virus Replication
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 10
    Publication Date: 2011-10-28
    Description: The dwarf planet Eris is a trans-Neptunian object with an orbital eccentricity of 0.44, an inclination of 44 degrees and a surface composition very similar to that of Pluto. It resides at present at 95.7 astronomical units (1 AU is the Earth-Sun distance) from Earth, near its aphelion and more than three times farther than Pluto. Owing to this great distance, measuring its size or detecting a putative atmosphere is difficult. Here we report the observation of a multi-chord stellar occultation by Eris on 6 November 2010 UT. The event is consistent with a spherical shape for Eris, with radius 1,163 +/- 6 kilometres, density 2.52 +/- 0.05 grams per cm(3) and a high visible geometric albedo, Pv = 0.96(+0.09)(-0.04). No nitrogen, argon or methane atmospheres are detected with surface pressure larger than approximately 1 nanobar, about 10,000 times more tenuous than Pluto's present atmosphere. As Pluto's radius is estimated to be between 1,150 and 1,200 kilometres, Eris appears as a Pluto twin, with a bright surface possibly caused by a collapsed atmosphere, owing to its cold environment. We anticipate that this atmosphere may periodically sublimate as Eris approaches its perihelion, at 37.8 astronomical units from the Sun.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sicardy, B -- Ortiz, J L -- Assafin, M -- Jehin, E -- Maury, A -- Lellouch, E -- Hutton, R Gil -- Braga-Ribas, F -- Colas, F -- Hestroffer, D -- Lecacheux, J -- Roques, F -- Santos-Sanz, P -- Widemann, T -- Morales, N -- Duffard, R -- Thirouin, A -- Castro-Tirado, A J -- Jelinek, M -- Kubanek, P -- Sota, A -- Sanchez-Ramirez, R -- Andrei, A H -- Camargo, J I B -- da Silva Neto, D N -- Gomes, A Ramos Jr -- Martins, R Vieira -- Gillon, M -- Manfroid, J -- Tozzi, G P -- Harlingten, C -- Saravia, S -- Behrend, R -- Mottola, S -- Melendo, E Garcia -- Peris, V -- Fabregat, J -- Madiedo, J M -- Cuesta, L -- Eibe, M T -- Ullan, A -- Organero, F -- Pastor, S -- de Los Reyes, J A -- Pedraz, S -- Castro, A -- de la Cueva, I -- Muler, G -- Steele, I A -- Cebrian, M -- Montanes-Rodriguez, P -- Oscoz, A -- Weaver, D -- Jacques, C -- Corradi, W J B -- Santos, F P -- Reis, W -- Milone, A -- Emilio, M -- Gutierrez, L -- Vazquez, R -- Hernandez-Toledo, H -- England -- Nature. 2011 Oct 26;478(7370):493-6. doi: 10.1038/nature10550.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉LESIA-Observatoire de Paris, CNRS, Universite Pierre et Marie Curie, Universite Paris-Diderot, 11, Rue Marcelin Berthelot, 92195 Meudon cedex, France. bruno.sicardy@obspm.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22031441" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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