Barrett, The Honors College Thesis/Creative Project Collection
Barrett, The Honors College at Arizona State University proudly showcases the work of undergraduate honors students by sharing this collection exclusively with the ASU community.
Barrett accepts high performing, academically engaged undergraduate students and works with them in collaboration with all of the other academic units at Arizona State University. All Barrett students complete a thesis or creative project which is an opportunity to explore an intellectual interest and produce an original piece of scholarly research. The thesis or creative project is supervised and defended in front of a faculty committee. Students are able to engage with professors who are nationally recognized in their fields and committed to working with honors students. Completing a Barrett thesis or creative project is an opportunity for undergraduate honors students to contribute to the ASU academic community in a meaningful way.
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Description
Microsolvation studies have begun to shed the light on the impact that single water molecules have on the structure of a molecule. The difference in behavior that molecules show when exposed to an increasing number of water molecules has been considered important but remains elusive. The cluster distributions of formic acid were studied for its known importance as an intermediate in the water gas shift reaction. Implementations of the water gas shift reaction range from a wide range of applications. Studies have proposed implementations such as variety such as making water on the manned mission to mars and as an industrial energy source. The reaction pathway of formic acid favors decarboxylation in solvated conditions but control over the pathway is an important field of study. Formic acid was introduced into a high vacuum system in the form of a cluster beam via supersonic expansion and was ionized with the second harmonic (400nm) of a pump-probe laser. Mass spectra showed a ‘magic’ 5,1 (formic acid, water) peak which showed higher intensity than was usually observed in clusters with 1 water molecule. Peak integration showed a higher relative abundance for the 5,1 cluster as well and showed the increased binding favorability of this conformation. As a result, there is an enhanced probability of molecules sticking together in this arrangement and this is due to the stable, cage-like structure that the formic acid forms when surrounding the water molecule.
ContributorsQuiroz, Lenin Mejia (Author) / Sayres, Scott G. (Thesis director) / Mills, Jeremy (Committee member) / Biegasiewicz, Kyle (Committee member) / School of Molecular Sciences (Contributor) / Barrett, The Honors College (Contributor)
Created2020-05
Description
Transient receptor potential (TRP) channels are a diverse family of polymodally gated nonselective cation channels implicated in a variety of pathophysiologies. Two channels of specific interest are transient receptor potential melastatin 8 (TRPM8) and transient receptor potential vanilloid 1 (TRPV1).
TRPM8 is the primary cold sensor in humans and is activated by ligands that feel cool such as menthol and icilin. It is implicated to be involved in a variety of cancers, nociception, obesity, addiction, and thermosensitivity. There are thought to be conserved regions of structural and functional importance to the channel which can be identified by looking at the evolution of TRPM8 over time. Along with this, looking at different isoforms of TRPM8 which are structurally very different but functionally similar can help isolate regions of functional interest as well. Between TRP channels, the transmembrane domain is well conserved and thought to be important for sensory physiology. To learn about these aspects of TRPM8, three evolutionary constructs, the last common primate, the last common mammalian, and the last common vertebrate ancestor TRPM8 were cloned and subjected to preliminary studies. In addition to the initial ancestral TRPM8 studies, fundamental studies were initiated in method development to evaluate the use of biological signaling sequences to attempt to force non-trafficking membrane protein isoforms and biophysical constructs to the plasma membrane. To increase readout for these and other studies, a cellular based fluorescence assay was initiated. Eventual completion of these efforts will lead to better understanding of the mechanism that underlie TRPM8 function and provide enhanced general methods for ion channel studies.
Beyond TRPM8 studies, an experiment was designed to probe mechanistic features of TRPV1 ligand activation. TRPV1 is also a thermosensitive channel in the TRP family, sensing heat and vanilloid ligands like capsaicin, commonly found in chili peppers. This channel is also involved in many proinflammatory interactions and associated with cancers, nociception, and addiction. Better understanding binding interactions can lead to attempts to create therapeutics.
TRPM8 is the primary cold sensor in humans and is activated by ligands that feel cool such as menthol and icilin. It is implicated to be involved in a variety of cancers, nociception, obesity, addiction, and thermosensitivity. There are thought to be conserved regions of structural and functional importance to the channel which can be identified by looking at the evolution of TRPM8 over time. Along with this, looking at different isoforms of TRPM8 which are structurally very different but functionally similar can help isolate regions of functional interest as well. Between TRP channels, the transmembrane domain is well conserved and thought to be important for sensory physiology. To learn about these aspects of TRPM8, three evolutionary constructs, the last common primate, the last common mammalian, and the last common vertebrate ancestor TRPM8 were cloned and subjected to preliminary studies. In addition to the initial ancestral TRPM8 studies, fundamental studies were initiated in method development to evaluate the use of biological signaling sequences to attempt to force non-trafficking membrane protein isoforms and biophysical constructs to the plasma membrane. To increase readout for these and other studies, a cellular based fluorescence assay was initiated. Eventual completion of these efforts will lead to better understanding of the mechanism that underlie TRPM8 function and provide enhanced general methods for ion channel studies.
Beyond TRPM8 studies, an experiment was designed to probe mechanistic features of TRPV1 ligand activation. TRPV1 is also a thermosensitive channel in the TRP family, sensing heat and vanilloid ligands like capsaicin, commonly found in chili peppers. This channel is also involved in many proinflammatory interactions and associated with cancers, nociception, and addiction. Better understanding binding interactions can lead to attempts to create therapeutics.
ContributorsShah, Karan (Author) / Van Horn, Wade (Thesis director) / Neisewander, Janet (Committee member) / Biegasiewicz, Kyle (Committee member) / School of Mathematical and Statistical Sciences (Contributor) / School of Molecular Sciences (Contributor, Contributor) / School of Life Sciences (Contributor) / Barrett, The Honors College (Contributor)
Created2020-05