Roger E. Koeppe
Affiliation confirmed via AI analysis of OpenAlex, ORCID, and web sources.
Distinguished Professor
Also affiliated: Oklahoma State University (1959–1979); California Institute of Technology (1975–1977); Argonne National Laboratory (2010); Centre National de la Recherche Scientifique (2000); Phoenix Houses of New England (2007); University of Leeds (2004); Johns Hopkins University (2002); University of Illinois Urbana-Champaign (1952); University of Tennessee Health Science Center (1953–1961); University of California, San Francisco (1961); Illinois Institute of Technology (2004); Utrecht University (1996–2008); Brookhaven National Laboratory (1984); University of Washington (1995); Cornell University (1986–2010); Kyoto University (1992); University of Michigan (2006); Abbott (United Kingdom) (1975); University of California San Diego (2008); University of Chicago (2010); Mount Sinai Medical Center (1961); Tri-Institutional PhD Program in Chemical Biology (2007); Max Planck Institute for Heart and Lung Research (1969); Johnson Foundation (1968); National Institute for Physiological Sciences (1995); Tenneco (United States) (1956); University of Missouri (2003); University of Pennsylvania (1968); Fairchild Semiconductor (United States) (1978–1979); Umeå University (1997–2007); Leipzig University (1998); Walter Reed Army Institute of Research (1975); Stanford University (1978–1985)
Faculty Researcher
Research Areas
Biomedical Subjects
Links
Biography and Research Information
OverviewAI-generated summary
Roger E. Koeppe's research focuses on the biophysical properties of lipid bilayers and their influence on the function of membrane proteins, particularly ion channels. His work investigates how intrinsic lipid curvature and bilayer elasticity modulate channel activity, employing single-molecule studies to explore these relationships. He also examines the complex interactions of gramicidins, a class of peptide antibiotics, within lipid environments, and studies the effects of specific amino acid residues, such as glutamic acid, on the structure and behavior of transmembrane helices embedded in membranes.
Koeppe leads a research group at the University of Arkansas at Fayetteville and has a notable publication record, with over 300 publications and more than 11,000 citations, reflected in his h-index of 55. He has collaborated with researchers such as Denise V. Greathouse at the University of Arkansas at Fayetteville and Jake R. Price at the University of Arkansas for Medical Sciences, co-authoring multiple publications with each. His work is recognized as high-impact, with recent activity and publications in 2024.
Metrics
- h-index: 55
- Publications: 309
- Citations: 11,227
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)
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Examination of pH dependency and orientation differences of membrane spanning alpha helices carrying a single or pair of buried histidine residues (2020)
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Membrane electrostatics sensed by tryptophan anchors in hydrophobic model peptides depends on non-aromatic interfacial amino acids: implications in hydrophobic mismatch (2020)
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Flanking aromatic residue competition influences transmembrane peptide helix dynamics (2020)
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Comparing Interfacial Trp, Interfacial His and pH Dependence for the Anchoring of Tilted Transmembrane Helical Peptides (2020)
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Influence of interfacial tryptophan residues on an arginine-flanked transmembrane helix (2019)
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Breaking the Backbone: Central Arginine Residues Induce Membrane Exit and Helix Distortions within a Dynamic Membrane Peptide (2019)
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Influence of Lipid Saturation, Hydrophobic Length and Cholesterol on Double‐Arginine‐Containing Helical Peptides in Bilayer Membranes (2019)
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Antidepressants are modifiers of lipid bilayer properties (2019)
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Transmembrane Helix Integrity versus Fraying To Expose Hydrogen Bonds at a Membrane–Water Interface (2018)
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Control of Transmembrane Helix Dynamics by Interfacial Tryptophan Residues (2018)
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Membrane Bending Moduli of Coexisting Liquid Phases Containing Transmembrane Peptide (2018)
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Helix formation and stability in membranes (2018)
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
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