Co-solvents can have profound effects on protein folding, self-assembly and hydrophobic collapse. Most such species are protein stabilizers that are believed to function by exclusion from the protein/water interface. Herein, we will discuss the correlation between sum frequency generation data and thermodynamic data taken  in the presence of stabilizing and destabilizing osmolytes. Data for water structure and osmolyte orientation will be compared with changes in surface tension at the air/water interface and the ability of the osmolytes to induce hydrophobic collapse of biopolymer molecules.

Alignment of osmolytes at hydrophobic and hydrophilic biointerfaces

244th National Meeting (2012)

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