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113 results on '"Kuschel, M."'

1. Experiments and Direct Numerical Simulations of binary collisions of miscible liquid droplets with different viscosities

Author

Focke, C., Bothe, D., Kuschel, M., and Sommerfeld, M.

Subjects
Physics - Fluid Dynamics, Computer Science - Computational Engineering, Finance, and Science
Abstract

Binary droplet collisions are of importance in a variety of practical applications comprising dispersed two-phase flows. The background of our research is the prediction of properties of particulate products formed in spray processes. To gain a more thorough understanding of the elementary sub-processes inside a spray, experiments and direct numerical simulations of binary droplet collisions are used. The aim of these investigations is to develop semi-analytical descriptions for the outcome of droplet collisions. Such collision models can then be employed as closure terms for scale-reduced simulations. In the present work we focus on the collision of droplets of different liquids. These kinds of collisions take place in every spray drying process when droplets with different solids contents collide in recirculation zones. A new experimental method has been developed allowing for high spatial and time resolved recordings via Laser-induced fluorescence. The results obtained with the proposed method will be compared with DNS simulations. The viscosities of the droplets are different whereas the interfacial tension and density are equal. The liquids are miscible and no surface tension is acting between the two liquids. Our intention is to discover elementary phenomena caused by the viscosity ratio of the droplets., Comment: 12th Triennial International Conference on Liquid Atomization and Spray Systems, Heidelberg, Germany, September 2-6, 2012

Published
2012

14. EMPOWER. Deliverable no 3.2 Business model methodology

Author

Kuschel, M., Weerdt, C.A. van der, Hjalmarsson, A., Amelsfort, D. van, and Alçenius, C.

Subjects
Mobility, HOI - Human Behaviour & Organisational Innovations, Traffic, Human & Operational Modelling, ELSS - Earth, Life and Social Sciences
Abstract

Based on EMPOWER Deliverable 3.1 and the use of complimenting resources, a Business Model Methodology is outlined in this deliverable in order to support and organize the work effort that should be performed to develop sound business models for the services that should be tested in four Living Lab Cities participating in the project. This deliverable includes an account how the methodology has driven the organization of the modelling work that will be performed at a later stage in the project and consequently provide input to both other tasks within WP3 as wells as tasks in other Work Packages.

Published
2015

17. Samverkansprojekt: Go:smart

Author

Strömdahl, A., Arby, H., Kuschel, M., Karlsson, M., Billger, M., Holmberg, P-E., A., Strömdahl., Strömdahl, A., Arby, H., Kuschel, M., Karlsson, M., Billger, M., Holmberg, P-E., and A., Strömdahl.

Abstract

Projektet Go:smart har haft som målsättning att utveckla och testa en innovativ tjänst för hållbara persontransporter i städer. Uppdraget var att göra vardagen lättare för storstads-hushåll och främja hållbara städer genom att erbjuda en enkel, flexibel och tillförlitlig prisvärd tjänst som ett alternativ till bilägandet. Projektet skulle också pröva möjligheten att elektrifiera kollektivtrafikfordon för att göra dessa attraktivare och därigenom bidra till att förbättra stadsutveckling och miljö., GO:SMART

Published
2014

42. Site-specific phosphorylation of a phospholamban peptide by cyclic nucleotide- and Ca2+/calmodulin-dependent protein kinases of cardiac sarcoplasmic reticulum.

Author

Karczewski, P., Kuschel, M., Baltas, L., Bartel, S., and Krause, E.

Abstract

Phospholamban (PLB), the regulator of the cardiac sarcoplasmic reticulum (SR) Ca2+ pump is specifically phosphorylated at Ser16 and Thr17 by cAMP-dependent protein kinase (PKA) and Ca2+/calmodulin-dependent protein kinase (CaMK), respectively. The regulation of this dual-site phosphorylation of amino acid residues in direct proximity is only poorly understood. In order to study the site-specific phosphorylation of PLB, we used a synthetic peptide (PLB-24) corresponding to the cytosolic part of the PLB monomer with the phosphorylation sites as a model substrate. PLB-24 possesses substrate properties as the native PLB as demonstrated by phosphorylation with exogenous, purified PKA, cGMP-dependent protein kinase (PKG) and a type II CaMK (CaMKII). In isolated vesicles of crdiac SR there was a rapid phosphorylation of the peptide by the endogenous PKA (SR-PKA) and CaMK (SR-CaMK), but not under conditions that activate PKG. Both SR-PKA and SR-CaMK incorporated the same amount of32P into PLB-24, 0.60±0.01 nmol32P/mg SR protein and 0.61±0.03 nmol32P/mg SR protein, respectively. Phosphorylation by SR-PKA was abolished by the specific PKA inhibitor (IC50=0.2μM), whereas SR-CaMK phosphorylation was inhibited by calmidazolium (IC50=1.6μM) and a CaMKII-specific inhibitor peptide (IC50=2.5μM). Phosphorylation by SR-PKA was exclusively at Ser, whereas SR-CaMK phosphorylated only Thr. After simultaneous activation of both SR-kinases32P incorporation into PLB-24 was additive and occurred at Ser as well as at Thr. Sequential activation of SR-PKA and SR-CaMK also caused the additive phosphorylation of PLB-24 independently of which kinase was activated first. Thus, at the monomeric level of PLB the respective phosphorylation site appears to be accessible to its related SR protein kinase in vitro even when the adjacent site is phosphorylated. [ABSTRACT FROM AUTHOR]

Published
1997
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43. G(i) protein-mediated functional compartmentalization of cardiac beta(2)-adrenergic signaling.

Author

Kuschel, M, Zhou, Y Y, Cheng, H, Zhang, S J, Chen, Y, Lakatta, E G, and Xiao, R P

Abstract

In contrast to beta(1)-adrenoreceptor (beta(1)-AR) signaling, beta(2)-AR stimulation in cardiomyocytes augments L-type Ca(2+) current in a cAMP-dependent protein kinase (PKA)-dependent manner but fails to phosphorylate phospholamban, indicating that the beta(2)-AR-induced cAMP/PKA signaling is highly localized. Here we show that inhibition of G(i) proteins with pertussis toxin (PTX) permits a full phospholamban phosphorylation and a de novo relaxant effect following beta(2)-AR stimulation, converting the localized beta(2)-AR signaling to a global signaling mode similar to that of beta(1)-AR. Thus, beta(2)-AR-mediated G(i) activation constricts the cAMP signaling to the sarcolemma. PTX treatment did not significantly affect the beta(2)-AR-stimulated PKA activation. Similar to G(i) inhibition, a protein phosphatase inhibitor, calyculin A (3 x 10(-8) M), selectively enhanced the beta(2)-AR but not beta(1)-AR-mediated contractile response. Furthermore, PTX and calyculin A treatment had a non-additive potentiating effect on the beta(2)-AR-mediated positive inotropic response. These results suggest that the interaction of the beta(2)-AR-coupled G(i) and G(s) signaling affects the local balance of protein kinase and phosphatase activities. Thus, the additional coupling of beta(2)-AR to G(i) proteins is a key factor causing the compartmentalization of beta(2)-AR-induced cAMP signaling.

Published
1999

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