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341 results on '"Saberi, Mohammad Reza"'

3. Monitoring Fluid Saturation in Reservoirs Using Time-Lapse Full-Waveform Inversion

Author

Mardan, Amir, Giroux, Bernard, Fabien-Ouellet, Gabriel, and Saberi, Mohammad Reza

Subjects
Physics - Geophysics
Abstract

Monitoring the rock-physics properties of the subsurface is of great importance for reservoir management. For either oil and gas applications or CO2 storage, seismic data are a valuable source of information for tracking changes in elastic properties which can be related to fluids saturation and pressure changes within the reservoir. Changes in elastic properties can be estimated with time-lapse full-waveform inversion. Monitoring rock-physics properties, such as saturation, with time-lapse full-waveform inversion is usually a two-step process: first, elastic properties are estimated with full-waveform inversion, then, the rock-physics properties are estimated with rock-physics inversion. However, multiparameter time-lapse full-waveform inversion is prone to crosstalk between parameter classes across different vintages. This leads to leakage from one parameter class to another, which, in turn, can introduce large errors in the estimated rock-physics parameters. To avoid inaccuracies caused by crosstalk and the two-step inversion strategy, we reformulate time-lapse full-waveform inversion to estimate directly the changes in the rock-physics properties. Using Gassmann's model, we adopt a new parameterization containing porosity, clay content, and water saturation. In the context of reservoir monitoring, changes are assumed to be induced by fluid substitution only. The porosity and clay content can thus be kept constant during time-lapse inversion. We compare this parameterization with the usual density-velocity parameterization for different benchmark models. Results indicate that the proposed parameterization eliminates crosstalk between parameters of different vintages, leading to more accurate estimation of saturation changes. We also show that using the parameterization based on porosity, clay content, and water saturation, the elastic changes can be monitored more accurately.

Published
2023
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28. Exploring the binding behavior mechanism of vitamin B12to α-Casein and β-Casein: multi-spectroscopy and molecular dynamic approaches

Author

Babayan-Mashhadi, Farahnaz, Rezvani-Noghani, Azadeh, Mokaberi, Parisa, Amiri-Tehranizadeh, Zeinab, Saberi, Mohammad Reza, and Chamani, Jamshidkhan

Abstract

AbstractThe aim of this study was to investigate the behavior interaction of α-Casein-B12and β-Casein-B12complexes as binary systems through the methods of multiple spectroscopic, zeta potential, calorimetric, and molecular dynamics (MD) simulation. Fluorescence spectroscopy denoted the role ofB12as a quencher in both cases of α-Casein and β-Casein fluorescence intensities, which also verifies the existence of interactions. The quenching constants of α-Casein-B12and β-Casein-B12complexes at 298 K in the first set of binding sites were 2.89 × 104and 4.41 × 104M−1, while the constants of second set of binding sites were 8.56 × 104and 1.58 × 105M−1, respectively. The data of synchronized fluorescence spectroscopy at Δλ = 60 nm were indicative of the closer location of β-Casein-B12complex to the Tyr residues. Additionally, the binding distance between B12and the Trp residues of α-Casein and β-Casein were obtained in accordance to the Förster’s theory of nonradioactive energy transfer to be 1.95 nm and 1.85 nm, respectively. Relatively, the RLS results demonstrated the production of larger particles in both systems, while the outcomes of zeta potential confirmed the formation of α-Casein-B12and β-Casein-B12complexes and approved the existence of electrostatic interactions. We also evaluated the thermodynamic parameters by considering the fluorescence data at three varying temperatures. According to the nonlinear Stern-Volmer plots of α-Casein and β-Casein in the presence of B12in binary systems, the two sets of binding sites indicated the detection of two types of interaction behaviors. Time-resolved fluorescence results revealed that the fluorescence quenching of complexes are static mechanism. Furthermore, the outcomes of circular dichroism (CD) represented the occurrence of conformational changes in α-Casein and β-Casein upon their binding to B12as the binary system. The experimental results that were obtained throughout the binding of α-Casein-B12and β-Casein-B12complexes were confirmed by molecular modeling.Communicated by Ramaswamy H. Sarma

Published
2024
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31. Investigating the analytical relationship between pore geometry and other pore space properties in carbonate rocks.

Author

Khadem, Benyamin, Saberi, Mohammad Reza, Krief, Michel, and Abbasi, Hossein Rezaei

Subjects
CARBONATE rocks, ROCK properties, ELASTICITY, GEOMETRY, GEOMETRIC modeling
Abstract

Although pore geometry plays an important role in carbonate rock physics modelling, few studies have been carried out on its analytic relationship with other pore space properties such as pore space stiffness. We propose an analytical workflow based on the differential effective medium (DEM) to estimate the elastic properties of carbonate rocks. The validity of our results is then cross-checked with the Xu and Payne model on a real carbonate dataset. This workflow establishes a direct and quantitative link between the pore geometry of carbonate rock and its other pore space properties such as the Biot coefficient and pore space stiffness. This relationship can, furthermore, be utilized in defining rock physics templates (RPTs) to investigate the role of pore geometry on the rock elastic properties. Furthermore, we extended the Biot–Gassmann–Krief (BGK) model through our proposed workflow by establishing a theoretical framework to relate the main components of the BGK model to the pore geometry usually estimated in the laboratory or empirically. This can help to investigate the impact of fluid substitution on each of these main components. Our investigation suggests that the higher the Biot and Gassmann coefficients, the more sensitive the rock is to fluid substitution. Moreover, this analytical workflow has been employed to examine the role of selecting different rotational spheroids (i.e. oblate and prolate) on the modelled velocities. Our results show that the modelled velocities depend on this selection in such a way that prolate pores are less sensitive to the variations in their pore aspect ratio compared with oblate pores. [ABSTRACT FROM AUTHOR]

Published
2024
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37. Structure, Function, and Physicochemical Properties of Pore-forming Antimicrobial Peptides

Author

Goki, Narjes Hosseini, Tehranizadeh, Zeinab Amiri, Saberi, Mohammad Reza, Khameneh, Bahman, and Bazzaz, Bibi Sedigheh Fazly

Abstract

Antimicrobial peptides (AMPs), a class of antimicrobial agents, possess considerable potential to treat various microbial ailments. The broad range of activity and rare complete bacterial resistance to AMPs make them ideal candidates for commercial development. These peptides with widely varying compositions and sources share recurrent structural and functional features in mechanisms of action. Studying the mechanisms of AMP activity against bacteria may lead to the development of new antimicrobial agents that are more potent. Generally, AMPs are effective against bacteria by forming pores or disrupting membrane barriers. The important structural aspects of cytoplasmic membranes of pathogens and host cells will also be outlined to understand the selective antimicrobial actions. The antimicrobial activities of AMPs are related to multiple physicochemical properties, such as length, sequence, helicity, charge, hydrophobicity, amphipathicity, polar angle, and also self-association. These parameters are interrelated and need to be considered in combination. So, gathering the most relevant available information will help to design and choose the most effective AMPs.

Published
2024
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39. Fabrication of versatile and sustainable cellulose nanocrystals from lettuce stalks as potential tamoxifen delivery vehicles for breast cancer treatment: biophysical, cellular and theoretical studies

Author

Khashkhashi-Moghadam, Sattar, primary, Soleimani, Samane, additional, Bazanjani, Aileen, additional, Hoseinpoor, Saeideh, additional, Taheri, Reza, additional, Mokaberi, Parisa, additional, Saberi, Mohammad Reza, additional, and Chamani, Jamshidkhan, additional

Published
2023
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42. Exploring the binding behavior mechanism of vitamin B12 to α-Casein and β-Casein: multi-spectroscopy and molecular dynamic approaches

Author

Babayan-Mashhadi, Farahnaz, Rezvani-Noghani, Azadeh, Mokaberi, Parisa, Amiri-Tehranizadeh, Zeinab, Saberi, Mohammad Reza, and Chamani, Jamshidkhan

Abstract

The aim of this study was to investigate the behavior interaction of α-Casein-B12 and β-Casein-B12 complexes as binary systems through the methods of multiple spectroscopic, zeta potential, calorimetric, and molecular dynamics (MD) simulation. Fluorescence spectroscopy denoted the role ofB12as a quencher in both cases of α-Casein and β-Casein fluorescence intensities, which also verifies the existence of interactions. The quenching constants of α-Casein-B12 and β-Casein-B12 complexes at 298 K in the first set of binding sites were 2.89 × 104 and 4.41 × 104 M−1, while the constants of second set of binding sites were 8.56 × 104 and 1.58 × 105 M−1, respectively. The data of synchronized fluorescence spectroscopy at Δλ = 60 nm were indicative of the closer location of β-Casein-B12 complex to the Tyr residues. Additionally, the binding distance between B12 and the Trp residues of α-Casein and β-Casein were obtained in accordance to the Förster’s theory of nonradioactive energy transfer to be 1.95 nm and 1.85 nm, respectively. Relatively, the RLS results demonstrated the production of larger particles in both systems, while the outcomes of zeta potential confirmed the formation of α-Casein-B12 and β-Casein-B12 complexes and approved the existence of electrostatic interactions. We also evaluated the thermodynamic parameters by considering the fluorescence data at three varying temperatures. According to the nonlinear Stern-Volmer plots of α-Casein and β-Casein in the presence of B12 in binary systems, the two sets of binding sites indicated the detection of two types of interaction behaviors. Time-resolved fluorescence results revealed that the fluorescence quenching of complexes are static mechanism. Furthermore, the outcomes of circular dichroism (CD) represented the occurrence of conformational changes in α-Casein and β-Casein upon their binding to B12 as the binary system. The experimental results that were obtained throughout the binding of α-Casein-B12 and β-Casein-B12 complexes were confirmed by molecular modeling. Communicated by Ramaswamy H. Sarma

Published
2023
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