Počet záznamů: 1
Cosolvent Exclusion Drives Protein Stability in Trimethylamine N-Oxide and Betaine Solutions
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SYSNO ASEP 0561273 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Cosolvent Exclusion Drives Protein Stability in Trimethylamine N-Oxide and Betaine Solutions Tvůrce(i) Ganguly, P. (US)
Bubák, D. (CZ)
Polák, J. (CZ)
Fagan, P. (CZ)
Dračínský, Martin (UOCHB-X) RID, ORCID
Van Der Vegt, N. F. A. (DE)
Heyda, J. (CZ)
Shea, J. E. (US)Zdroj.dok. Journal of Physical Chemistry Letters. - : American Chemical Society - ISSN 1948-7185
Roč. 13, č. 34 (2022), s. 7980-7986Poč.str. 7 s. Jazyk dok. eng - angličtina Země vyd. US - Spojené státy americké Klíč. slova force-field ; preferential interactions ; glycine betaine Obor OECD Atomic, molecular and chemical physics (physics of atoms and molecules including collision, interaction with radiation, magnetic resonances, Mössbauer effect) CEP GA22-15374S GA ČR - Grantová agentura ČR Způsob publikování Omezený přístup Institucionální podpora UOCHB-X - RVO:61388963 UT WOS 000864672500001 EID SCOPUS 85137136902 DOI 10.1021/acs.jpclett.2c01692 Anotace Using a combination of molecular dynamics simulation, dialysis experiments, and electronic circular dichroism measurements, we studied the solvation thermodynamics of proteins in two osmolyte solutions, trimethylamine N-oxide (TMAO) and betaine. We showed that existing force fields are unable to capture the solvation properties of the proteins lysozyme and ribonuclease T1 and that the inaccurate parametrization of protein-osmolyte interactions in these force fields promoted an unphysical strong thermal denaturation of the trpcage protein. We developed a novel force field for betaine (the KBB force field) which reproduces the experimental solution Kirkwood-Buff integrals and density. We further introduced appropriate scaling to protein-osmolyte interactions in both the betaine and TMAO force fields which led to successful reproduction of experimental protein-osmolyte preferential binding coefficients for lysozyme and ribonuclease T1 and prevention of the unphysical denaturation of trpcage in osmolyte solutions. Correct parametrization of protein-TMAO interactions also led to the stabilization of the collapsed conformations of a disordered elastin-like peptide, while the uncorrected parameters destabilized the collapsed structures. Our results establish that the thermodynamic stability of proteins in both betaine and TMAO solutions is governed by osmolyte exclusion from proteins. Pracoviště Ústav organické chemie a biochemie Kontakt asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Viktorie Chládková, Tel.: 232 002 434 Rok sběru 2023 Elektronická adresa https://doi.org/10.1021/acs.jpclett.2c01692
Počet záznamů: 1