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Biomolecular Simulations Group

Dylan Ogden

Dylan Ogden


Dylan Ogden, current third year graduate student, received his Bachelor of Science in Chemistry (emphasis in Biochemistry) from the University of Arkansas in Spring of 2017. He enjoys spending time with friends and family and refining his grilling/bbq skills.


Membrane Protein Conformational Dynamics in Glucose Transporter 1

GluT1, a human uniporter belonging to the sugar porter subfamily of MFS (Major Facilitator Superfamily) transporters, mediates the uptake of glucose by passively transporting it along its concentration gradient. GluT1 is one of the most extensively studied membrane transport proteins. Due to this a number of mutations, deficits, and overexpression in malignent cells has been determined. We have conducted an extensive study of GluT1 comparing the apo and glucose bound systems with systems of each containing the protonation of a number of different residues.

Exploration of the Conformational Transition Pathway of GkPOT

GkPOT (Geobacillus kaustophilus), a Proton-coupled oligopeptide transporters (POTs) is among the symporter members of the MFS superfamily. POTs uptake small peptides and peptide like molecules to the cell across the cell membrane using the inward directed proton electrochemical gradient as the source of energy for their active symport function. A very important feature among POTs is substrate promiscuity attributed to the binding site accommodating a range of peptides and peptide like molecules in multiple orientations. To explore the transition pathway of GkPOT we utilize a series of nonequlibrium simulation techniques to compare an apo and dialanine bound systems.

Copyright © 2015, Biomolecular Simulations Group, Department of Chemistry and Biochemistry, University of Arkansas.
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