Specific ion effects on protein interfaces have been observed for many years, but yet comprehensive explanations regarding the mechanism by which ions interact with proteins and more general aqueous interfaces are still under investigation. Realistically, ion specificity on protein stability is due to numerous contributions and interactions between the solution and protein. However, the most important contribution is arguably the hydrophobic effect, specifically the change in free energy when water molecules are liberated from the interfacial region upon protein folding. In the work presented here, the effects of different ions on the critical micelle concentration (CMC) of 1, 2 –Hexanediol were examined to study salt effects on hydrophobicity by the means of fluorescence spectroscopy. Our results show that anions and cations do exhibit the specific effects on hydrophobic interactions. However, the origin of these specific ion effects different for cations and anions. Cation specific effects are caused by their ability to form cavities in solution, while anion specific effects arise from their ability to interact with the interface. These results are of interest to the researchers in the protein folding field, providing significant experimental hydrophobicity data necessary for theoretical biologists that are attempting to predict protein structures. / February 2015
| Identifer | oai:union.ndltd.org:MANITOBA/oai:mspace.lib.umanitoba.ca:1993/30135 |
| Date | 18 December 2014 |
| Creators | Sorokina, Olga |
| Contributors | Khajehpour, Mazdak (Chemistry), McKenna, Sean (Chemistry) Mark, Brian (Microbiology) |
| Source Sets | University of Manitoba Canada |
| Detected Language | English |
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