The Role of Hydrophobic Interactions in the Swelling of Elastin
The volume of water-swollen elastin varies dramatically with temperature, and it has been suggested that this swelling behaviour is due to changes in the strength of hydrophobic interactions between the numerous non-polar groups in the elastin protein. In this study Flory-Rehner Theory for network swelling has been used to test this hypothesis and to determine if hydrophobic interactions alone can quantitatively account for the observed volume changes. Calculated values for the solvent-polymer interaction parameter, χl derived from swelling data have been compared with independent values for the free energy of interaction between water and non-polar groups. Results indicate that the swelling changes can be attributed entirely to changes in the hydration of non-polar groups. Presumably, peptide groups and other polar regions are fully hydrated under all conditions studied.
KeywordsHydrophobic Interaction Free Energy Change Random Network Polymer Segment Elastic Mechanism
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