General Mechanism of Osmolytes’ Influence on Protein Stability Irrespective of the Type of Osmolyte Cosolvent - Publication - Bridge of Knowledge

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General Mechanism of Osmolytes’ Influence on Protein Stability Irrespective of the Type of Osmolyte Cosolvent

Abstract

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.

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Category:
Articles
Type:
artykuł w czasopiśmie wyróżnionym w JCR
Published in:
JOURNAL OF PHYSICAL CHEMISTRY B no. 120, edition 43, pages 11159 - 11169,
ISSN: 1520-6106
Language:
English
Publication year:
2016
Bibliographic description:
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:
Digital Object Identifier (open in new tab) 10.1021/acs.jpcb.6b10119
Verified by:
Gdańsk University of Technology

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