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Mechanism of Osmolyte Stabilization–Destabilization of Proteins: Experimental Evidence

Abstrakt

In this work, we investigated the influence of stabilizing (N,N,N-trimethylglycine) and destabilizing (urea) osmolytes on the hydration spheres of biomacromolecules in folded forms (trpzip-1 peptide and hen egg white lysozyme─hewl) and unfolded protein models (glycine─GLY and N-methylglycine─NMG) by means of infrared spectroscopy. GLY and NMG were clearly limited as minimal models for unfolded proteins and should be treated with caution. We isolated the spectral share of water changed simultaneously by the biomacromolecule/model molecule and the osmolyte, which allowed us to provide unambiguous experimental arguments for the mechanism of stabilization/destabilization of proteins by osmolytes. In the case of both types of osmolytes, the decisive factor determining the equilibrium folded/unfolded state of protein was the enthalpy effect exerted on the hydration spheres of proteins in both forms. In the case of stabilizing osmolytes, enthalpy was also favored by entropy, as the unfolded state of a protein was more entropically destabilized than the folded state.

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Wersja publikacji
Accepted albo Published Version
DOI:
Cyfrowy identyfikator dokumentu elektronicznego (otwiera się w nowej karcie) 10.1021/acs.jpcb.2c00281
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Creative Commons: CC-BY otwiera się w nowej karcie

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Informacje szczegółowe

Kategoria:
Publikacja w czasopiśmie
Typ:
artykuły w czasopismach
Opublikowano w:
JOURNAL OF PHYSICAL CHEMISTRY B nr 126, strony 2990 - 2999,
ISSN: 1520-6106
Język:
angielski
Rok wydania:
2022
Opis bibliograficzny:
Stasiulewicz M., Panuszko A., Bruździak P., Stangret J.: Mechanism of Osmolyte Stabilization–Destabilization of Proteins: Experimental Evidence// JOURNAL OF PHYSICAL CHEMISTRY B -Vol. 126,iss. 16 (2022), s.2990-2999
DOI:
Cyfrowy identyfikator dokumentu elektronicznego (otwiera się w nowej karcie) 10.1021/acs.jpcb.2c00281
Źródła finansowania:
Weryfikacja:
Politechnika Gdańska

wyświetlono 115 razy

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