Have you ever wondered…
How particles affect climate?
How alcohol is toxic to the liver?
How laser light affects molecules?
How natural products are synthesized?
How green experiments are developed?
These and many other perplexing questions are being investigated every day at Hendrix College.
Explore below the diverse research projects being conducted in the Chemistry Department or
have a look at the research being conducted by our graduates.
Undergraduate Research Opportunities
The Caro Research Group is interested in the biochemical mechanisms by which alcoholic beverages produce liver damage. We use cell fractions (endoplasmic reticulum, mitochondria), cells (liver cells in culture), and experimental animals
(mice), and analytical, biological, and cellular chemical techniques including HPLC, polarography, real time PCR, RT-PCR, ELISA, western blot, chemiluminescence, fluorimetry, spectrometry, flow cytometry, and fluorescence microscopy.
Dr. Gron’s research interests presently include environmental sampling of water and soil, development of undergraduate chemical educational materials: green analytical laboratories and scientific literacy, and the analysis of biologically relevant ions: hydrogen sulfide/garlic project.
Dr. Bill Gunderson’s research is in the field of
bioinorganic chemistry. Research in the Gunderson group has two aims: 1)
determine the role of manganese in biomacromolecules, including enzymes and DNA
structures, and 2) develop low-cost instrumentation for biochemical
and biophysical studies. The first aim includes investigations of the enzyme,
toxoflavin lyase, a Mn-containing enzyme that helps protect rice crops from
bacterial infections. These enzymatic studies include enzyme kinetics and
active site-structure studies using electron paramagnetic resonance (EPR)
spectroscopy and other spectroscopic methods. Dr. Gunderson is also
investigating the binding characteristics of Mn to DNA hairpins and three-way
DNA junctions using EPR spectroscopy. The second aim includes
developing spectroscopic techniques using 3D printing technology and Arduino
Methods of mass spectrometry are used to study
the energetics and dynamics of peptide folding and reactivity. Specifically,
this includes relative energies of different conformations, energy barriers to
conformational changes, and thermodynamics of activation for certain
reactions. Ion mobility spectrometry-mass spectrometry (IMS-MS) separates
and detects different conformations of the same molecule in the gas
phase. Ion trap mass spectrometry (ITMS) quantifies the ions in a sample
by mass and charge. Together, these methods allow us to follow processes
in solution or in the gas phase. This work is a collaboration with
scientists at Indiana University, where the IMS-MS instrumentation is
located. ITMS experiments, data analysis, and modeling are performed at
The Hatch Research Group uses an integrative and multidisciplinary approach to study the effects of natural aerosols on the Earth system. We aim to better understand how natural aerosol influences atmospheric chemistry
and climate. Currently, we are working on two ongoing research projects. The first project combines theoretical and experimental results to predict the cloud condensation nuclei (CCN) activity of natural insoluble aerosols from water adsorption measurements on mineral dusts and volcanic ash using Fourier Transform Infrared (FT-IR) spectroscopy. The second project aims to explore the chemical composition of atmospheric aerosols using a high-volume aerosol sampler for collection of particles, followed by chemical characterization using ion chromatography (IC) and gas chromatography/mass spectrometry (GC/MS)
In the Kett Research
Group we are interested in studying surface and interfacial phenomena.
Specifically we look at how solid surfaces interact with adsorbed molecules and
how the adsorption process can be controlled through changes in ionic strength,
pH, and surface charge. Currently the group is focused on developing a kinetic
model for the formation of supported lipid bilayers (SLBs) on a silicon dioxide
(SiO2) surface. SLBs are a class of model biological membrane in
which a phospholipid bilayer is supported on a metal or non-metal surface. They
are used as mimics of biological cell membranes as the large number of
different molecules that are in a cell membrane makes it difficult to determine
the structure, dynamics and interactions of each individual membrane component.
Although SLBs can be formed on a number of different surfaces, they do not form
on all surfaces and it is not usually possible to make an a priori
prediction as to whether a particular combination of phospholipid
concentration, surface, salt concentration, temperature, and solution pH will
result in the formation of an SLB. By monitoring the real time formation of
SLBs using a Quartz Crystal Microbalance (QCM) we are developing a mechanistic
model that will allow us to determine how each of these experimental conditions
affects the formation of SLBs.
one-third of medication approved by the Federal Drug Administration targets a
family of proteins called the G protein-coupled receptors (GPCRs). GPCRs are
located in the cellular membranes and are responsible for activating internal
cellular pathways in response to external cellular stimuli. GPCRs are potential
targets for medication that aims to treat obesity, depression, and chronic
pain. Despite the recent advances in protein-structure determination,
GPCR-targeted drug design proves to be difficult because GPCRs are very
flexible and dynamic, and different structures can elicit different cellular
responses. The focus of this research is to use computational techniques to
predict the most energetically favorable structures at different activation states
in order to design drugs that bind to and stabilize those conformations. Our
lab uses Schrodinger software to optimize and minimize protein structures
before running molecular dynamics of the proteins in a solvated and neutralized
cellular bilayer at physiological temperature and pressure to sample protein
conformational space. Once the most stable structure is identified, software
programs such as DockBlaster and MTIOpenScreen search libraries of
commercially-available small molecules to identify known compounds that can
potentially bind to and stabilize our protein conformations in a desired
activation state. The selected ligands are then docked to the proteins using
Glide software, where the binding energies are calculated. We identify
compounds that can potentially bind to GPCRs, such as the cannabinoid and
opioid receptors, in order to treat diseases such as chronic pain and