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dc.contributor.supervisor Khajehpour, Mazdak (Chemistry) en_US
dc.contributor.author Beauchamp, David L
dc.date.accessioned 2012-04-13T15:24:06Z
dc.date.available 2012-04-13T15:24:06Z
dc.date.issued 2012-04-13
dc.identifier.uri http://hdl.handle.net/1993/5306
dc.description.abstract It has long been observed that salts affect proteins in a variety of ways, yet comprehensive explanations for different salt effects are still lacking. In the work presented here, the effect of salts on proteins has been investigated through three different effects: the hydrophobic effect; their conformational stability; the hydrogen bonding network of water in a protein’s hydration shell. UV-vis absorbance and fluorescence spectroscopy were used to monitor changes in two model systems, the phenol-acetate contact pair and the model enzyme ribonuclease t1. It was shown that salts affect the hydrophobicity of the contact pair according to their charge density, induced image charges play an important role in the observed salt-induced increase of ribonuclease t1 stability, and that salts affect ribonuclease t1 activity through modulation of the hydrogen bonds of water in the enzyme’s hydration shell. This work contributes a greater understanding of the effect of salts on proteins. en_US
dc.subject Hydrophobic effect en_US
dc.subject Fluorescence quenching en_US
dc.subject Salt effects en_US
dc.subject Protein folding en_US
dc.subject Induced point-image charges en_US
dc.subject Kirkwood interactions en_US
dc.subject Continuum model en_US
dc.subject Hydrogen bonding en_US
dc.subject Water-water interactions en_US
dc.subject Charge density en_US
dc.subject Enzymatic activity en_US
dc.title The Effect of Salts on the Conformational Stability of Proteins en_US
dc.degree.discipline Chemistry en_US
dc.contributor.examiningcommittee Mark, Brian (Microbiology); McKenna, Sean (Chemistry); Perreault, Hélène (Chemistry) en_US
dc.degree.level Master of Science (M.Sc.) en_US
dc.description.note May 2012 en_US


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