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 (drlivesa@uncc.edu). And now that I have
gotten the ball rolling, hopefully others will also contribute a blog entry
summarizing their work.
Happy researching,
-- Dr. Livesay, Coordinator of the CRS program
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