A student researcher in the biochemistry labs

At Mount Holyoke I have been able to engage with my professors and peers in meaningful discussion of course material and have been encouraged to pursue my own interests in the field.

Major: Biochemistry

Research Group: McMenimen Lab

In my research in Dr. McMenimen’s laboratory we are characterizing small heat shock proteins (sHsps), members of the chaperone family of proteins, named aptly for their activation by cellular stress such as heat. sHsps are known for their dynamic nature and constant change in oligomeric states.

The dimer is proposed to be the smallest active oligomer with chaperone activity and a building block for larger oligomers. Understanding the dimer will give us critical insight into the mechanism of sHsps in health, such how they help keep eye lenses clear, and to their role in diseases such as cataracts.

I specifically seek to design, synthesize, and characterize two constructs fusing a sHsps with glutathione s-transferase (GST), which will allow us to study the dimers of GST-Hsp27 and GST-CRYAB (crystalline, alpha B). After purification of the chimeric protein from BL21 E. coli cells using size exclusion chromatography I perform western blotting using native and denaturing conditions to ensure that the protein is intact with both the GST and sHsps and so I can confirm the presence of dimers.

In order to characterize the chaperone activity we are optimizing a variety of assays including, UV/Visible spectroscopy, CD spectroscopy, and a gel chaperone assay. My chemistry and biochemistry background has prepared me for conducting research by providing me with information that I can apply, and laboratory techniques that I use in my research. More importantly Mount Holyoke has given me the confidence in being able to independently find information and solve problems.

At Mount Holyoke I have been able to engage with my professors and peers in meaningful discussion of course material and have been encouraged to pursue my own interests in the field.