Roger E. Koeppe Data-verified
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Distinguished Professor
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Biography and Research Information
OverviewAI-generated summary
Roger E. Koeppe, Distinguished Professor at the University of Arkansas at Fayetteville, investigates the molecular mechanisms governing ion channel function within lipid bilayers. His research group focuses on how the biophysical properties of cell membranes, such as intrinsic lipid curvature and bilayer elasticity, influence the behavior and regulation of ion channels. This work involves comparative single-molecule studies to understand these complex interactions.
Koeppe's recent publications explore the role of specific amino acid residues, like glutamic acid, in modulating the properties of transmembrane helices and their interaction with lipid environments. He also studies the complexing properties of gramicidins, a class of peptide antibiotics known for forming ion channels in biological membranes. His scholarly contributions are reflected in a high h-index of 55, over 312 publications, and more than 11,000 citations, designating him as a highly cited researcher. He has collaborated with Denise V. Greathouse at the University of Arkansas at Fayetteville and Jake R. Price at the University of Arkansas for Medical Sciences.
Metrics
- h-index: 55
- Publications: 310
- Citations: 11,178
Selected Publications
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Intrinsic Lipid Curvature and Bilayer Elasticity as Regulators of Channel Function: A Comparative Single-Molecule Study (2024)
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Illuminating Disorder Induced by Glu in a Stable Arg-Anchored Transmembrane Helix (2021)
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Lipid-Dependent Titration of Glutamic Acid at a Bilayer Membrane Interface (2021)
Collaboration Network
Top Collaborators
- Lipid-Dependent Titration of Glutamic Acid at a Bilayer Membrane Interface
- Illuminating Disorder Induced by Glu in a Stable Arg-Anchored Transmembrane Helix
- Lipid-Dependent Titration of Glutamic Acid at a Bilayer Membrane Interface
- Illuminating Disorder Induced by Glu in a Stable Arg-Anchored Transmembrane Helix
- Lipid-Dependent Titration of Glutamic Acid at a Bilayer Membrane Interface
- Lipid-Dependent Titration of Glutamic Acid at a Bilayer Membrane Interface
- Illuminating Disorder Induced by Glu in a Stable Arg-Anchored Transmembrane Helix
- Intrinsic Lipid Curvature and Bilayer Elasticity as Regulators of Channel Function: A Comparative Single-Molecule Study
- Intrinsic Lipid Curvature and Bilayer Elasticity as Regulators of Channel Function: A Comparative Single-Molecule Study
- Complexing Properties of Gramicidins
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