Postdoctoral Research Scientist
Using flurorescence spectroscopy to study ion channels in a native, membrane environment.
ATP-sensitive K+ channels (KATP) couple metabolism to cellular excitability. This important physiological process is governed by binding of intracellular adenine nucleotides (ATP/ADP) to three types of site on the channel complex. After decades of study, the details of nucleotide handling by KATP remain obscure.
However, understanding nucleotide regulation remains an important goal because KATP is crucial for
insulin secretion, and mutations that disrupt this regulation result in diabetes or hyperinsulinism.
I use a combination of fluorescence spectroscopy and electrophysiology to study intact KATP tagged with a fluorescent non-canonical amino acid and expressed in cellular membranes. Using these approaches, I am investigating ligand binding to KATP (in particular how each binding site contributes to channel opening/closing) and the conformational changes that occur subsequent to ligand binding to influence channel gating.
Cryo-electron microscopy structures and progress toward a dynamic understanding of KATP channels.
Puljung MC., (2018), J gen physiol, 150, 653 - 669
The Nucleotide-Binding Sites of SUR1: A Mechanistic Model.
Vedovato N. et al, (2015), Biophys j, 109, 2452 - 2460
New structural insights into the gating movements of CFTR.
Puljung MC., (2015), J gen physiol, 145, 365 - 369
Dynamic measurements for funny channels.
Puljung MC., (2014), Proc natl acad sci u s a, 111, 14320 - 14321