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• W330286904 endingPage "250" @default.
• W330286904 startingPage "183" @default.
• W330286904 abstract "The contributions of the polar and nonpolar components of the proteins and nucleic acids can be regarded as constituting the bricks and mortar, respectively, of the two structures. This chapter describes the changes in enthalpy and entropy of reactions as diverse as denaturation, ligand binding, and self-association display a characteristic dependence on temperature, which is not evident in the free energy changes. The chapter focuses on comparing the energetic data on protein reactions with similar data on model systems to evaluate the contributions of the various groups to the thermodynamic parameters of protein reactions. The folding of the proteins is different from that of the nucleic acids, because the energetics of the interactions with water of the nonpolar side chains and bases are different, and owing to the planarity and partial polar properties of the purine and pyrimidine bases, they cluster by forming stacks. The thermodynamic parameters responsible for polypeptide folding are similar to those found for other protein reactions—that is, ligand binding, or subunit association, because they are controlled by the interactions of the same groups with water. The stability of the folded conformations is controlled largely by the interactions of the nonpolar side chains of the amino acids and the purine and pyrimidine bases with water. Although, nucleic acids do not show the low-temperature dissociation found with numerous protein aggregates, however, they show only positive values for these two functions." @default.
• W330286904 created "2016-06-24" @default.
• W330286904 creator A5044208902 @default.
• W330286904 creator A5072787877 @default.
• W330286904 date "1976-01-01" @default.
• W330286904 modified "2023-09-27" @default.
• W330286904 title "The Thermodynamic Basis of the Stability of Proteins, Nucleic Acids, and Membranes" @default.
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