General Mechanism of Osmolytes’ Influence on Protein Stability Irrespective of the Type of Osmolyte Cosolvent
Abstrakt
The stability of proteins in an aqueous solution can be modified by the presence of osmolytes. The hydration sphere of stabilizing osmolytes is strikingly similar to the enhanced hydration sphere of a protein. This similarity leads to an increase in the protein stability. Moreover, the hydration sphere of destabilizing osmolytes is significantly different. These solutes generate in their surroundings so-called “structurally different water”. The addition of such osmolytes causes “dissolution” of the specific protein hydration sphere and destabilizes its folded form. No relationship is seen between the stabilizing/destabilizing properties of osmolytes and their structure-making/-breaking influence on water. Furthermore, their accumulation at the protein surface or their exclusion does not determine the osmolytes’ effect on protein stability. An explanation to the osmolytes’ stabilizing/destabilizing influence originates in the similarity of water properties in osmolytes and protein solutions. The spectral infrared characteristic of water in an osmolyte solution allowed us to develop practical criteria for classifying solutes as stabilizing or destabilizing agents.
Cytowania
-
5 8
CrossRef
-
0
Web of Science
-
5 7
Scopus
Autorzy (4)
Cytuj jako
Pełna treść
pełna treść publikacji nie jest dostępna w portalu
Słowa kluczowe
Informacje szczegółowe
- Kategoria:
- Publikacja w czasopiśmie
- Typ:
- artykuł w czasopiśmie wyróżnionym w JCR
- Opublikowano w:
-
JOURNAL OF PHYSICAL CHEMISTRY B
nr 120,
wydanie 43,
strony 11159 - 11169,
ISSN: 1520-6106 - Język:
- angielski
- Rok wydania:
- 2016
- Opis bibliograficzny:
- Panuszko A., Bruździak P., Kaczkowska E., Stangret J.: General Mechanism of Osmolytes’ Influence on Protein Stability Irrespective of the Type of Osmolyte Cosolvent// JOURNAL OF PHYSICAL CHEMISTRY B. -Vol. 120, iss. 43 (2016), s.11159-11169
- DOI:
- Cyfrowy identyfikator dokumentu elektronicznego (otwiera się w nowej karcie) 10.1021/acs.jpcb.6b10119
- Weryfikacja:
- Politechnika Gdańska
wyświetlono 226 razy