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- W2024941431 abstract "Abstract It is proposed that changes in the hydrophobic contribution to the free energy of a protein in aqueous solution can be considered in terms of alterations in the hydrophobic interfacial free energy due to adsorption of solutes; the latter parameter is coupled with the net surface area of hydrophobic groups exposed to the aqueous phase. This concept is utilised to estimate the change in the hydrophobic contribution to the free energy of native lysozyme caused by the addition of quaternary ammonium bromide homologues of varying hydrophobicity and thereby predict the resultant changes in the temperature ( T m ) of thermal denaturation. At a given concentration of free solute, the change in T m is proportional to the change in the surface tension (γ) of an air-water or oil-water interface. For example, KCI and tetramethylammonium bromide increase T m and γ while 0.5 M and 1.0 M tetraethylammonium bromide, tetrapropylammonium bromide and tetrabutylammonium bromide decrease both parameters in the ratio 1:3:8. Predictions of the absolute values of alterations in T m can be made using the differences between the surface area of hydrophobic groups exposed to solvent in the native and random coil forms of lysozyme. Agreement between theory and experiment is only achieved if it is assumed, in agreement with previous studies, that many hydrophobic groups are still buried in the heat-denatured form of lysozyme. In order to advance on the semi-quantitative agreement between theory and experiment reported here, the conformations of denatured protein molecules need elucidating in more detail." @default.
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- W2024941431 date "1977-11-01" @default.
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- W2024941431 title "Hydrophobic free energy and the denaturation of proteins" @default.
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- W2024941431 doi "https://doi.org/10.1016/0005-2795(77)90245-8" @default.
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