The impact of denaturing and stabilizing osmolytes on protein conformational dynamics has been extensively explored due to the significant contribution of protein solvation to the stability, function, malfunction and regulation of globular proteins. We studied the effect of two nonspecific organic molecules, urea, which is a conventional denaturant, and dimethyl sulfoxide (DMSO), which is a multilateral organic solvent, on the stability and conformational dynamics of a non-inhibitory serpin, ovalbumin (OVA). A differential scanning microcalorimetry (DSC) experimental series conducted in the phosphate buffer solutions containing 0–30% of additives revealed the destabilizing impact of both urea and DMSO in a mild acidic media, manifested in the gradual decrease of thermal unfolding enthalpy and transition temperature. These findings differ from the results observed in our study of the mild alkaline DMSO buffered solutions of OVA, where the moderate stabilization of OVA was observed in presence of 5–10% of DMSO. However, the overall OVA interaction patterns with urea and DMSO are consistent with our previous findings on the stability and conformational flexibility of another model globular protein, α-chymotrypsin, in similar medium conditions. The obtained results could be explained by preferential solvation patterns. Positive preferential solvation of protein by urea in urea/water mixtures mainly weakens the hydrophobic interactions of the protein globule and eventually leads to the disruption of the tertiary structure within the whole range of urea concentrations. Alternatively, under certain experimental conditions in DMSO/water mixtures, positive preferential solvation by water molecules can be observed. We assume that the switch to the positive preferential solvation by DMSO, which is shown to have a soft maximum around 20–30% DMSO, could be shifted towards lower additive concentrations due to the intrinsic capability of ovalbumin OVA to convert into a heat-stable, yet flexible set of conformations that have increased the surface hydrophobicity, characteristic to molten-globule-like states.
Citation: Tatyana Tretyakova, Maya Makharadze, Sopio Uchaneishvili, Mikhael Shushanyan, Dimitri Khoshtariya. Exploring the role of preferential solvation in the stability of globular proteins through the study of ovalbumin interaction with organic additives[J]. AIMS Biophysics, 2023, 10(4): 440-452. doi: 10.3934/biophy.2023025
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The impact of denaturing and stabilizing osmolytes on protein conformational dynamics has been extensively explored due to the significant contribution of protein solvation to the stability, function, malfunction and regulation of globular proteins. We studied the effect of two nonspecific organic molecules, urea, which is a conventional denaturant, and dimethyl sulfoxide (DMSO), which is a multilateral organic solvent, on the stability and conformational dynamics of a non-inhibitory serpin, ovalbumin (OVA). A differential scanning microcalorimetry (DSC) experimental series conducted in the phosphate buffer solutions containing 0–30% of additives revealed the destabilizing impact of both urea and DMSO in a mild acidic media, manifested in the gradual decrease of thermal unfolding enthalpy and transition temperature. These findings differ from the results observed in our study of the mild alkaline DMSO buffered solutions of OVA, where the moderate stabilization of OVA was observed in presence of 5–10% of DMSO. However, the overall OVA interaction patterns with urea and DMSO are consistent with our previous findings on the stability and conformational flexibility of another model globular protein, α-chymotrypsin, in similar medium conditions. The obtained results could be explained by preferential solvation patterns. Positive preferential solvation of protein by urea in urea/water mixtures mainly weakens the hydrophobic interactions of the protein globule and eventually leads to the disruption of the tertiary structure within the whole range of urea concentrations. Alternatively, under certain experimental conditions in DMSO/water mixtures, positive preferential solvation by water molecules can be observed. We assume that the switch to the positive preferential solvation by DMSO, which is shown to have a soft maximum around 20–30% DMSO, could be shifted towards lower additive concentrations due to the intrinsic capability of ovalbumin OVA to convert into a heat-stable, yet flexible set of conformations that have increased the surface hydrophobicity, characteristic to molten-globule-like states.
differential scanning calorimetry;
ovalbumin;
S-ovalbumin;
dimethyl sulfoxide;
α-chymotrypsin
In most of the countries, the solar photovoltaic systems have reached to the grid parity. The higher capacity of solar photovoltaic power plants are connecting within the higher and medium voltage networks, and lower capacity photovoltaic units within the low voltage network (i.e., distributed network). There are many technical challenges for integrating the solar PV plants at higher voltage levels as well as lower voltage levels. The key challenging issues, for increasing further penetration of solar photovoltaic systems in the electrical power network, are technology developments for intelligent power conditioning devices, integration of hybrid energy storage for making solar photovoltaic system as dispatchable power source, mitigation of power quality issues, demand side management, technology development of solar photovoltaic based micro-grid, techno-economic operational strategies, etc.
The solar photovoltaic system engineering depends on many factors (e.g., techno-economic sizing, energy management, energy dispatch strategies, resources allocations etc.). Different geographical locations as well as climatic conditions also influence the operation and performance of the solar photovoltaic-based system. The incident solar radiation has significant impact on the solar photovoltaic system energy production. The solar photovoltaic system energy output is influenced by the geometrical configuration of photovoltaic array and the view factor to sky effect. In the recent years, there are many technical innovations, developments have happened for deployments of solar photovoltaic system grid integration with energy storage for participating either as an active generator or operating as a solar photovoltaic based micro-grid. Within the distributed energy network, solar photovoltaic systems can also be used as ‘building integrated photovoltaic systems (BIPV)’ to provide electrical energy locally and make the buildings as ‘zero energy buildings (ZEBs)’. In future, ZEBs are going to play a significant role in the upcoming smart distributed energy network development due to their contribution of on-site electrical generation through solar photovoltaic systems, energy storage, demand side management etc. In order to increase further PV penetration within the distribution network and develop innovative mitigation techniques, there is critical need of further field-oriented research in the above-mentioned topics.
This Special Issue of AIMS Energy Journal comprises peer-review articles on advancement of power dispatching techniques for solar photovoltaic system with energy storage, shading and diffused solar radiation effects on the performance of solar photovoltaic system, intelligent controllers for distributed energy resources allocations, material characterization for heterojunction solar cells. In addition, some articles cover the typical case studies of solar photovoltaic systems in the tropical region.
As the Guest Editor of this Special Issue ‘Solar Photovoltaic System Engineering’ of the AIMS Energy Journal, I express my sincere appreciation to the journal editorial team, authors and reviewers of the manuscripts, journal editorial supporting team, and all those who have contributed and supported in successful fruition and publication.
Professor Mohan Lal Kolhe
Professor in Smart Grid and Renewable Energy
Faculty of Engineering and Science,
University of Agder,
PO Box 422, NO 4604, Kristiansand, Norway
E-mail: Mohan.L.Kolhe@uia.no
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Figures(3) / Tables(1)
Tatyana Tretyakova, Maya Makharadze, Sopio Uchaneishvili, Mikhael Shushanyan, Dimitri Khoshtariya. Exploring the role of preferential solvation in the stability of globular proteins through the study of ovalbumin interaction with organic additives[J]. AIMS Biophysics, 2023, 10(4): 440-452. doi: 10.3934/biophy.2023025
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