Mateusz Marek Nowak
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Previous Organizations / Institutes
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Mateusz Marek Nowak has a total of 1 co-authors. Here are the top co-authors by number of shared publications:
- Michał Spirzewski
National Centre for Nuclear Research, ul. Andrzeja Sołtana 7, 05-400 Otwock-Świerk, Poland
1 shared publication
Latest Publications
- Open Access
A Similarity-Based Scaling Methodology for the Thermal-Hydraulic Design of Dual Fluid Reactor Demonstrators
The Dual Fluid Reactor (DFR) is a Generation IV concept that relies on a phased development pathway using a low-temperature microdemonstrator (DEMO) and a high-temperature minidemonstrator (mDEMO). A rigorous methodology is required to scale experimental data between these facilities to ensure the reliable design of the final reactor. This paper establishes such a methodology grounded in Similarity Theory. The Cathare-2 system code was used to perform a parametric study on a simplified model of the demonstrators, which use lead–bismuth eutectic and pure liquid lead, respectively. This study focused on identifying the specific operating conditions required to match key “defining” dimensionless numbers—the Reynolds number (Re) for dynamic similarity and the Peclet number (Peh) for thermal similarity. The analysis successfully identified and presented the distinct operating ranges of fluid velocity and mass flow required to achieve either state. Results show that matching the Reynolds number allows for the dimensionless pressure drop to be scaled with a deviation below 0.2%, while matching the Peclet number allows for the dimensionless temperature profile to be scaled with a deviation under 2.5%. The central finding is that dynamic and thermal similarity cannot be achieved simultaneously due to the different working fluids and temperatures of the demonstrators. This forces a strategic choice in experimental design, where an experiment must be tailored to investigate either fluid dynamics or heat transfer. This work provides the foundational “rulebook” for designing these crucial experiments, ensuring that data from the DFR demonstrator program is both reliable and scalable.Open AccessA Similarity-Based Scaling Methodology for the Thermal-Hydraulic Design of Dual Fluid Reactor Demonstrators
The Dual Fluid Reactor (DFR) is a Generation IV concept that relies on a phased development pathway using a low-temperature microdemonstrator (DEMO) and a high-temperature minidemonstrator (mDEMO). A rigorous methodology is required to scale experimental data between these facilities to ensure the reliable design of the final reactor. This paper establishes such a methodology grounded in Similarity Theory. The Cathare-2 system code was used to perform a parametric study on a simplified model of the demonstrators, which use lead–bismuth eutectic and pure liquid lead, respectively. This study focused on identifying the specific operating conditions required to match key “defining” dimensionless numbers—the Reynolds number (Re) for dynamic similarity and the Peclet number (Peh) for thermal similarity. The analysis successfully identified and presented the distinct operating ranges of fluid velocity and mass flow required to achieve either state. Results show that matching the Reynolds number allows for the dimensionless pressure drop to be scaled with a deviation below 0.2%, while matching the Peclet number allows for the dimensionless temperature profile to be scaled with a deviation under 2.5%. The central finding is that dynamic and thermal similarity cannot be achieved simultaneously due to the different working fluids and temperatures of the demonstrators. This forces a strategic choice in experimental design, where an experiment must be tailored to investigate either fluid dynamics or heat transfer. This work provides the foundational “rulebook” for designing these crucial experiments, ensuring that data from the DFR demonstrator program is both reliable and scalable. - 20 February 2004
- Published by Wiley in Proteins: Structure, Function, and Bioinformatics
- Vol. 55 (1) , 11-21
Immunoglobulin kappa light chain and its amyloidogenic mutants: A molecular dynamics study
AL amyloidosis and LCDD are pathological conditions caused by extracellural deposition of monoclonal Ig light chain variable domains. In the former case, deposits have a form of amyloid fibrils, in the latter, amorphous aggregates. 1REI κ light chain variable domain and its two point mutants, R61N and D82I, were chosen for the analysis in this work. Wild 1REI does not create deposits in vitro, while R61N aggregates as amyloid fibrils and D82I creates amorphous aggregates. Both mutated residues create a conserved salt bridge; thus, substitution of any of them should decrease VL domain stability. For these three proteins, 5 ns MD simulations were conducted in temperatures of 300 K and 400 K, with protonated and unprotonated acidic residues, mimicking acidic and neutral experimental pH conditions (3 sets: N300, N400, and A400). The analysis of trajectories focused on characterization of changes in conformational behavior and stability of Ig κ light chain variable domain caused by single aminoacid substitutions that were experimentally proved to enhance aggregation propensity, both in the form of amyloid and amorphous aggregates. Residue D82 turns out to be involved not only in R61–D82 but also in K45–D82 interaction, which was not observed in the X‐ray structure, but frequently populated simulations of 1REI. The substitution D82I excludes both interactions, resulting in substantial destabilization (i.e., easier aggregation). Examination of behavior of edge regions of VL β‐sandwich reveals significant alterations in D82I mutant compared to wild 1REI, while relatively small changes occur in R61N. This suggests that mild and slow destabilization is the reason of the conversion of VL to partially folded amyloidogenic intermediate structure. Proteins 2004.
- 20 February 2004
- Published by Wiley in Proteins: Structure, Function, and Bioinformatics
- Vol. 55 (1) , 11-21
Immunoglobulin kappa light chain and its amyloidogenic mutants: A molecular dynamics study
AL amyloidosis and LCDD are pathological conditions caused by extracellural deposition of monoclonal Ig light chain variable domains. In the former case, deposits have a form of amyloid fibrils, in the latter, amorphous aggregates. 1REI κ light chain variable domain and its two point mutants, R61N and D82I, were chosen for the analysis in this work. Wild 1REI does not create deposits in vitro, while R61N aggregates as amyloid fibrils and D82I creates amorphous aggregates. Both mutated residues create a conserved salt bridge; thus, substitution of any of them should decrease VL domain stability. For these three proteins, 5 ns MD simulations were conducted in temperatures of 300 K and 400 K, with protonated and unprotonated acidic residues, mimicking acidic and neutral experimental pH conditions (3 sets: N300, N400, and A400). The analysis of trajectories focused on characterization of changes in conformational behavior and stability of Ig κ light chain variable domain caused by single aminoacid substitutions that were experimentally proved to enhance aggregation propensity, both in the form of amyloid and amorphous aggregates. Residue D82 turns out to be involved not only in R61–D82 but also in K45–D82 interaction, which was not observed in the X‐ray structure, but frequently populated simulations of 1REI. The substitution D82I excludes both interactions, resulting in substantial destabilization (i.e., easier aggregation). Examination of behavior of edge regions of VL β‐sandwich reveals significant alterations in D82I mutant compared to wild 1REI, while relatively small changes occur in R61N. This suggests that mild and slow destabilization is the reason of the conversion of VL to partially folded amyloidogenic intermediate structure. Proteins 2004.