Research
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.
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