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Understanding the interactions between protein stabilizers and the peptide bond through the analysis of the volumetric and compressibility properties for the model systems

Abstract

This work confirms our earlier supposition, that volumetric and acoustic parameters for simple model proposed by us are directly related to stabilizing/destabilizing effect of osmolytes on proteins structure. The apparent molar volumes, V and the apparent molar isentropic compressions, KS,, of glycine and N,N,N –trimethylglycine (betaine) were determined from densities and speed of sound measurements in aqueous solution of N-methylacetamide (as a model of peptide bond of protein). The standard molar parameters for osmolytes were obtained from concentration dependence of the calculated quantities at NMA concentration equal 2, 4, 6 and 8 (mol/kg) and at temperature T = (288.15, 298.15 and 308.15) K. The standard values were combined with volumetric and compressibility data for amino acids in pure water to obtain transfer properties from water to aqueous N-methylacetamide solutions. The standard partial molar volume of transfer of studied osmolytes, 〖Δ_t V〗_Φ^0, seems to be related mainly to hydrophilic/hydrophobic features of molecules. The stabilizing/destabilizing effect of solute on protein structure is reflected in temperature influence on the limiting partial molar quantities.

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Category:
Articles
Type:
artykuły w czasopismach
Published in:
JOURNAL OF CHEMICAL THERMODYNAMICS no. 160,
ISSN: 0021-9614
Language:
English
Publication year:
2021
Bibliographic description:
Kaczkowska E., Wawer J., Tyczyńska M., Jóźwiak M., Krakowiak J.: Understanding the interactions between protein stabilizers and the peptide bond through the analysis of the volumetric and compressibility properties for the model systems// JOURNAL OF CHEMICAL THERMODYNAMICS -Vol. 160, (2021), s.106485-
DOI:
Digital Object Identifier (open in new tab) 10.1016/j.jct.2021.106485
Verified by:
Gdańsk University of Technology

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