PREDICTION OF THERMODYNAMIC INSTABILITIES OF PROTEIN SOLUTIONS FROM SIMPLE PROTEIN-PROTEIN INTERACTIONS
| Autor: | Antonio Emanuele, Tommaso D'Agostino, J. R. Solana |
|---|---|
| Přispěvatelé: | D'Agostino, T, Solana, JR, Emanuele, A, D’Agostino, T, Solana, J, D'Agostino, Tommaso, Solana, José Ramón, Emanuele, Antonio |
| Jazyk: | angličtina |
| Rok vydání: | 2012 |
| Předmět: |
Quantitative Biology::Biomolecules
Spinodal Range (particle radiation) Liquid–liquid demixing Spinodal line Chemistry Solvent mediated protein-protein interaction Enthalpy Protein solution General Physics and Astronomy Thermodynamics Entropy driven phase transition Liquid-liquid demixing Action (physics) Settore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin) Solvent mediated protein–protein interaction Protein–protein interaction Spinodal lines SW potential free energy parametrization Physics and Astronomy (all) Mean field theory Finite potential well Molecule Physical and Theoretical Chemistry Square well potential |
| Popis: | Statistical thermodynamics of protein solutions is often studied in terms of simple, microscopic models of particles interacting via pairwise potentials. Such modelling can reproduce the short range structure of protein solutions at equilibrium and predict thermodynamics instabilities of these systems. We introduce a square well model of effective protein-protein interaction that embeds the solvent's action. We modify an existing model [45] by considering a well depth having an explicit dependence on temperature, i.e. an explicit free energy character, thus encompassing the statistically relevant configurations of solvent molecules around proteins. We choose protein solutions exhibiting demixing upon temperature decrease (lysozyme, enthalpy driven) and upon temperature increase (haemoglobin, entropy driven). We obtain satisfactory fits of spinodal curves for both the two proteins without adding any mean field term, thus extending the validity of the original model. Our results underline the solvent role in modulating or stretching the interaction potential. © 2013 Elsevier B.V. All rights reserved. |
| Databáze: | OpenAIRE |
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