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Sure I guess I can start this with a brief explanation of what I do.

I'm a PhD Candidate in Chemical Biology at the University of Michigan. My work focuses on developing methods for the detection of chemical modifications on proteins to increase our understanding of the role of these modifications in diseases such as cancer and neurodegeneration.

Quick Background:
The central dogma of molecular biology (Im sure you're somewhat familiar with this if you have taken a Biology class) is that DNA encodes genetic information which is read by RNA and translated in to the production of proteins. Proteins are the workhorses of the cell and do almost all of the work such as carrying out and regulating biochemical processes such as metabolism, signaling, tissue differentiation, etc. Basically if a cell does it, proteins are the things making it happen.

There are only about 25,000 genes in human DNA which encodes for about 100,000 proteins, but due to the vast diversity in functions required by the cell, these proteins have to be chemically modified (after being made) to carry out their specific tasks which creates more than 1 million possible types of proteins in a cellular environment. These modifications can act as on/off switches, can direct the proteins to specific locations in the cell, and much more.

As you might expect, understanding the state of each protein in a cell at any given moment can provide incredible insight into how cells function and how diseases such as cancer take root. However, with more than 1million possible forms of proteins, detecting each and every one of them at the same time is a monumental task.

The good news is that we now have technology that is capable of detecting a huge number of proteins and we work with other labs who create software to delve into the massive data sets and provide usable information.

So this is where my lab comes in.

My project works specifically with a modification that is involved in trafficking proteins (how proteins know where to go) to the cellular membrane, and between cellular compartments. This is achieved through the chemical addition/ removal of a fatty acid to specific proteins which are needed near the surface of the cell such as those involved in cell to cell adhesion or involved in signalling events such as cell growth. If these modifications are not regulated carefully cells can break away from tissues or grow out of control. This is exactly why cancers (cancer= unregulated cell growth) can become metastatic (or detached from a tumor and grow in other organs). Currently there is no way to directly detect exactly which proteins have these modifications on a cellular wide scale. So we are working on improving methods of determining which proteins are modified in this manner and how they contribute to the overall regulation of these events.

Now WAKE UP!
The test will be tomorrow....
 
We will also collect, Lu-Hf isotopic ratios which helps us trace the evolution of the zircon crystal with regards to a mantle magma source (where in the mantle the rock was created) and helps to link the host rock evolution to plate tectonic settings. We will use the trace element composition data in the zircons to determine petrogenetic processes occurring as the zircon crystallized, again indicating a plate tectonic setting of origin. When these data are combined we can compare it to known, previously described terranes to determine a possible origin for the Marshfield terrane.
So my understanding of the mantle is that it is fluidic and an essentially homogenous layer. Is this untrue? If you can trace the origins of magma then there must be some signature to mantle regions that implies distinct heterogeneity?
 
I sucked at college bio, so I sincerely apologize if I misunderstood, but are you suggesting that if you could remove specific fatty acids from specific proteins, it could potentially stop cancer cell amalgamation? (assuming you could find the right protein and acid)
Youre on the right track.
Its really more of a matter of determining which mutations prevent proper regulation of these fatty acid modifications. For instance we know a particular protein mutant causes cancer. The protein is regulated through this modification and is important for signalling growth. In cancer it won't stop signalling for growth. We know it has this modification, so we hope that we can now target this and determine whether by preventing fatty acylation we can kill the cancer.

It's quite the opposite for metastasis, where mutations prevent fatty acid addition and therefore cause the proteins to mislocalize. They arent on the cell surface and therefore cannot be there to attach to other proteins on adjacent cells and break away.

So really it's a sensitive balance of fatty acid modification regulation that needs to be studied
 
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