TitleImpact of Small Organic Molecules on The Stability and Conformational Flexibility of Globular Proteins |
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AuthorsDr. Tatyana Tretyakova, Lepl I. Beritashvili Center of Experimental Biomedicine, GeorgiaDr. Maya Makharadze, Lepl I. Beritashvili Center of Experimental Biomedicine, Georgia Dr. Sophio Uchaneishvili, Lepl I. Beritashvili Center of Experimental Biomedicine, Georgia Dr. Dimitri Khoshtariya, Lepl I. Beritashvili Center of Experimental Biomedicine, Georgia |
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AbstractProfound understanding of mechanisms governing proteins’ function is one of the major goals of both fundamental and applied biomedical sciences. Recent theoretical and experimental studies showed that protein function is essentially linked to its structure, stability and conformational flexibility, which in turn can be drastically altered by the crowded intracellular environment of proteins. The aim of presented research is to investigate an impact of nonspecific organic additives, urea and dimethyl sulfoxide (DMSO), on the conformational properties of model globular protein, hen egg albumin (HEA). We applied differential scanning microcalorimetry to measure thermodynamic parameters of HEA thermal unfolding in presence of wide range of additives concentrations. Our resent experiment revealed that HEA exhibited gradual destabilization in whole range of buffered urea solutions (0-30% urea in PSB, pH8.0), manifested through monotonic decrease of melting temperature and significant decrease of enthalpy which is not concentration dependant within the experimental range of concentrations. However, in presence of the same concentrations of DMSO (PSB, pH8.0), we observed slight increase of the melting temperature and enthalpy in 5% DMSO solution, followed by gradual decrease of both thermodynamic parameters with increase of DMSO concentration. Experimental results obtained for interaction of HEA with DMSO are qualitatively similar to our previous findings on α-chymotrypsin and could be explained by change of preferential solvation of water against DMSO, which was never observed in denaturizing urea solutions. Low concentrations of DMSO remotely strengthen bond water networks of the protein protecting it from unfolding, whereas subsequent increase of DMSO concentration leads to gradual destabilization of the protein. This work was supported by Shota Rustaveli National Science Foundation of Georgia (SRNSFG) grant YS-18-2034 and is a part of systematic fundamental research on the intrinsic links between protein stability, conformational flexibility and function. |
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Keywordsprotein stability, differential scanning calorimetry, urea, dimethyl sulfoxide |
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CitationTretyakova, T., Makharadze, M., Uchaneishvili, S. & Khoshtariya, D. (2020). Impact of Small Organic Molecules on The Stability and Conformational Flexibility of Globular Proteins. In V. M. Bradley & I. Sahin (Eds.), Proceedings of iLSET 2020--International Conference on Life Sciences, Engineering and Technology (pp. 30-32). Monument, CO, USA: ISTES Organization. Retrieved 21 November 2024 from 2020.ilset.net/proceedings/5/. |
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