I do not have any actual CRS scholars working in my lab this summer, but I do have two undergrads doing research with me right now so I thought I would quickly summarize their projects. My lab is broadly focused on elucidating the mechanisms that underlie protein function. Proteins are large biological macromolecules that do nearly everything within a cell -- they catalyze chemical reactions, provide structural and mechanical support, relay signals, and are intimately involved in countless additional tasks. In fact, there is not a single biological process that I can think of that is not directly or indirectly affected by proteins.
Due to their size, proteins have interesting shapes (see picture), and the traditional dogma states that these shapes define their function. This is mostly true; however, shape alone is not the whole story. Rather, proteins (like all molecules) have intramolecular motions, what Richard Feynman famously called the “…jigglings and wigglings of atoms." My lab is trying to understand how these motions are related to function. Moreover, we want to determine if these motions are conserved across groups of evolutionarily and/or functionally related proteins.
While experimental methods to characterize protein motions exist, they are expensive and time-consuming. As such, our “microscope” is a computer, and we spend much of our time developing computer code to simulate dynamical properties of proteins. This process requires expertise in chemistry, physics, and computer science, which is typically too much to ask of an undergrad. As such, my undergrad students are working on the application of our model to two different biomedically important proteins. Specifically:
-- Christian Russell (a student from Greensboro College) is working with NDM-1, which is New Delhi metallo-beta-lactamase-1. This is the enzyme that confers antibiotic resistance to a particularly virulent strain of bacteria that led to a number of patient deaths recently. This work is just piece of a larger puzzle that my lab has been working on. That is, we are trying to determine if differences in dynamical properties across the beta-lactamase family can explain antibiotic resistance activities.
-- Mike Ross (a UNC Charlotte student) is working on GAT, which is the GABA-transporter protein. GAT’s function is to clear out the neurotransmitter GABA from the synapse, thus terminating its signal. While not as famous as neurotransmitters like serotonin or adrenaline, GABA is involved in over 40% of all inhibitory processes and altered GABAergic transmission is associated with a number of pathologies, including epilepsy, anxiety, and pain.
So, that’s a snapshot of what we are working on this summer. Visit my website for more information (http://coitweb.uncc.edu/~drlivesa/), or feel free to email me with questions (firstname.lastname@example.org). And now that I have gotten the ball rolling, hopefully others will also contribute a blog entry summarizing their work.
-- Dr. Livesay, Coordinator of the CRS program