Abstract
Proteins are stabilised by the difference between the bond energies between interacting amino acids and the energy of interaction between these amino acids and water (several MJ∕mol each). Protein folding decreases not only the enthalpy, but also the entropy of the molecule. Hence the total stabilisation energy is ≈ 20–60kJ∕mol which should be compared with thermal energy k T ( ≈ 2kJ∕mol at room temperature).
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Buxbaum, E. (2011). Folding and Unfolding of Proteins. In: Biophysical Chemistry of Proteins. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-7251-4_35
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DOI: https://doi.org/10.1007/978-1-4419-7251-4_35
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