Hydration of lysozyme: the protein-protein interface and the enthalpy-entropy compensation

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Hydration of lysozyme: the protein-protein interface and the enthalpy-entropy compensation

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Publication Article, peer reviewed scientific
Title Hydration of lysozyme: the protein-protein interface and the enthalpy-entropy compensation
Author(s) Kocherbitov, Vitaly ; Arnebrant, Thomas
Date 2010
English abstract
Water sorption isotherms of proteins are usually interpreted with such models as BET or GAB that imply the formation of multilayers at solid-gas interface. However, this approach is not applicable to globular proteins such as humid lysozyme where a solid-gas interface does not exist. Another popular approach is the D’Arcy-Watt model, where besides the formation of multilayers the heterogeneity of energies of sorption sites of proteins is taken into account. Here we present sorption calorimetric data on the hydration of lysozyme that confirms the existence of the heterogeneity. The magnitude of the heterogeneity is, however, lower than one can expect on the basis of the existence of a solid-gas interface. Moreover, the calorimetric data show a strong enthalpy-entropy compensation that leads to almost constant effective free energy of hydration in the activity range normally used for fitting the data to sorption models. This allows the use of the Langmuir equation for the fitting of the initial part of the sorption isotherm of lysozyme. Assuming the formation of a monolayer of water at the protein-protein interface, one can estimate the size of the lysozyme molecules from the sorption isotherm. The result of this estimation is in good agreement with the structural data on lysozyme, which supports the presented approach.
DOI http://dx.doi.org/10.1021/la903210e (link to publisher's fulltext)
Publisher ACS
Host/Issue Langmuir;6
Volume 26
ISSN 0743-7463
Pages 3918-3922
Language eng (iso)
Subject(s) sorption
calorimetry
Sciences
Research Subject Categories::NATURAL SCIENCES::Chemistry::Physical chemistry::Surface and colloid chemistry
Research Subject Categories::NATURAL SCIENCES::Chemistry::Physical chemistry::Biophysical chemistry
Research Subject Categories::NATURAL SCIENCES::Chemistry::Physical chemistry
Handle http://hdl.handle.net/2043/9180 (link to this page)

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