DR WAND'S LAB GROUP

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• Our lab broadly focusses on the thermodynamics (specifically entropy) of intermembrane protein molecular recognition. Intermembrane proteins are typically very difficult to express and purify, and thus there is a dearth of knowledge about not only intermembrane proteins in general but also the thermodynamics of these proteins. 

• The folding and molecular recognition of soluble proteins is well-known: soluble proteins do not have very high conformational entropy due to the energy offset that the hydrophobic effect provides. But since the chemistry of integral membrane proteins happens within the hydrophobic membrane, this hydrophobic effect is not present. 

• It has been shown in two very different intermembrane proteins (pSRII and OmpW) that there is a significantly higher conformational entropy than every soluble protein characterized, thus, it is proposed that this might exist as a trend across all intermembrane proteins.

Year 1: My Sophomore Year

• I expressed and purified three different proteins over the course of Fall 2022 and Spring 2023:

  • BCL-XL: an antiapoptotic protein of the BCL-2 family localized in the mitochondria. BCL-XL interacts with VDAC-1 to inhibit mitochondrial mediated apoptosis, as well as interacting with other mitochondrial membrane proteins to mediate other cellular functions. The protein is essential for the protection of neurons, as well as its role in transporting Ca+2 to the mitochondria and increasing ATP production.​

  • VDAC-1: a proapoptotic protein involved in regulation of cell metabolism and spermatogenesis. The overexpression of this protein is affiliated with many different diseases, including cancer, dementia, Alzheimer's, type II diabetes, lupus, and other autoimmune diseases. 

  • MSP-1D1: a membrane scaffolding protein used in the creation of nanodisks, in which membrane proteins are inserted into for the study of their structure and dynamics using NMR.

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Year 2: My Junior Year

• I focused on expressing and purifying the integral membrane protein GlpG. Specifically, I focused on streamlining a purification protocol for future studies of GlpG. Although the cellular role of GlpG in E. coli isn't fully known, it's an important protein to study due to its uniqueness as an integral membrane protein: GlpG is protease (a protein that degrades other proteins, using water as a nucleophile) and an integral membrane protein. Since there is no water in the plasma membrane, and since there is a lack of research into the dynamics of intermembrane proteases, GlpG provides a fairly unique model protein that could provide inside not only into protease thermodynamics but also intermembrane protein dynamics in general.

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Summer 2024:

• At the point of writing this (July), I have overexpressed GlpG in recombinant cells and then purified the protein 5 separate times. Although we've never achieved a satisfactory purity, we think we're getting close to solving the issue. Hopefully the next time I update this page we'll have been able to fully purify GlpG