Our laboratory treats bulk water as a direct participant in protein folding equilibria. This leads to the hypothesis that small solutes that perturb the bulk phase may influence protein folding or stability without directly contacting the protein. In other words, we aim to develop a new thermodynamic framework that opposes the theory of preferential interactions, as commonly cited for interpreting solute effects.

• Performed wet-lab on the binding interactions between molecules using isothermal titration calorimetry(ITC) and microscale thermophoresis (MST)

• Analyzed working solutions using Ultraviolet-Visible Spectroscopy (UV-Vis)

• Worked closely with graduate-level students involving their project involved in quantifying the desolvation energy between DNA related systems.

• Prepared reports on research methodology and conclusions

• Prepared stock buffer solutions

• Standardized pH meters and kept daily logs for instruments.

• Maintained cleanliness and organization in laboratory areas

Experienced in using other lab equipment in a Biochemist lab such as Differential Scanning Calorimeter (DSC), Density Meter, HP model 8452A Diode Array Spectrometer, Sonicator, Incubator, Centrifuge, and Circular Dichroism Spectra (CD).