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); University of Leeds (2004–2007); Université Libre de Bruxelles (2001); Johns Hopkins University (2002); Max Planck Society (1969); University of Illinois Urbana-Champaign (1952); 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); University of Tennessee System (1957–1959); University of Arkansas System (2007); Johns Hopkins Medicine (2002); University of California San Diego (2008); University of Oxford (2003–2010); University of Chicago (2010); Abbott (United States) (1975); Max Planck Institute for Heart and Lung Research (1969); Centre for Biomedical Engineering and Physics (2007); University of California San Francisco Medical Center (1961); Max Planck Institute for Biophysical Chemistry (1998); Stanford Medicine (1978–1985); Centre de recherche Paul Pascal (2000); National Institute for Physiological Sciences (1995); Instituto Superior Técnico (2008); Weill Cornell Medicine (2000–2010); University of Missouri (2003); University of Coimbra (2008); University of Pennsylvania (1968); Rockefeller University (2007); Umeå University (1996–2007); Leipzig University (1998); Walter Reed Army Institute of Research (1975); University of Memphis (1953–1961); Stanford University (1978–1985)
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: 308
- Citations: 11,598
Positions
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Distinguished Professor 1979–presentUniversity of Arkansas Fayetteville Chemistry & Biochemistry ORCID
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
- Different Membrane Anchoring Positions of Tryptophan and Lysine in Synthetic Transmembrane α-Helical Peptides
- Induction of Nonbilayer Structures in Diacylphosphatidylcholine Model Membranes by Transmembrane α-Helical Peptides: Importance of Hydrophobic Mismatch and Proposed Role of Tryptophans
- Regulation of Sodium Channel Function by Bilayer Elasticity
- Influence of Lipid/Peptide Hydrophobic Mismatch on the Thickness of Diacylphosphatidylcholine Bilayers. A 2H NMR and ESR Study Using Designed Transmembrane α-Helical Peptides and Gramicidin A
- The Preference of Tryptophan for Membrane Interfaces
Showing 5 of 54 shared publications
- Bilayer Thickness and Membrane Protein Function: An Energetic Perspective
- Bilayer-dependent inhibition of mechanosensitive channels by neuroactive peptide enantiomers
- Regulation of Sodium Channel Function by Bilayer Elasticity
- Kinetics of Gramicidin Channel Formation in Lipid Bilayers: Transmembrane Monomer Association
- Docosahexaenoic acid alters bilayer elastic properties
Showing 5 of 41 shared publications
- Different Membrane Anchoring Positions of Tryptophan and Lysine in Synthetic Transmembrane α-Helical Peptides
- Induction of Nonbilayer Structures in Diacylphosphatidylcholine Model Membranes by Transmembrane α-Helical Peptides: Importance of Hydrophobic Mismatch and Proposed Role of Tryptophans
- Influence of Lipid/Peptide Hydrophobic Mismatch on the Thickness of Diacylphosphatidylcholine Bilayers. A 2H NMR and ESR Study Using Designed Transmembrane α-Helical Peptides and Gramicidin A
- Tilt Angles of Transmembrane Model Peptides in Oriented and Non-Oriented Lipid Bilayers as Determined by 2H Solid-State NMR
- Geometry and Intrinsic Tilt of a Tryptophan-Anchored Transmembrane α-Helix Determined by 2H NMR
Showing 5 of 13 shared publications
- Buried lysine, but not arginine, titrates and alters transmembrane helix tilt
- Changes in Transmembrane Helix Alignment by Arginine Residues Revealed by Solid-State NMR Experiments and Coarse-Grained MD Simulations
- Charged or Aromatic Anchor Residue Dependence of Transmembrane Peptide Tilt
- Comparison of “Polarization Inversion with Spin Exchange at Magic Angle” and “Geometric Analysis of Labeled Alanines” Methods for Transmembrane Helix Alignment
- Tyrosine Replacing Tryptophan as an Anchor in GWALP Peptides
Showing 5 of 13 shared publications
- Hydrophobic Coupling of Lipid Bilayer Energetics to Channel Function
- Importance of Tryptophan Dipoles for Protein Function: 5-Fluorination of Tryptophans in Gramicidin A Channels
- Energetics of Heterodimer Formation among Gramicidin Analogues with an NH2-terminal Addition or Deletion
- On the helix sense of gramicidin A single channels
- Modulation of Gramicidin Channel Structure and Function by the Aliphatic “Spacer” Residues 10, 12, and 14 between the Tryptophans
Showing 5 of 9 shared publications
- Tilt Angles of Transmembrane Model Peptides in Oriented and Non-Oriented Lipid Bilayers as Determined by 2H Solid-State NMR
- Geometry and Intrinsic Tilt of a Tryptophan-Anchored Transmembrane α-Helix Determined by 2H NMR
- Hydrophobic Mismatch between Helices and Lipid Bilayers
- Orientation and Motion of Tryptophan Interfacial Anchors in Membrane-Spanning Peptides
- Helical Distortion in Tryptophan- and Lysine-Anchored Membrane-Spanning α-Helices as a Function of Hydrophobic Mismatch: A Solid-State Deuterium NMR Investigation Using the Geometric Analysis of Labeled Alanines Method
Showing 5 of 8 shared publications
- Comparison of “Polarization Inversion with Spin Exchange at Magic Angle” and “Geometric Analysis of Labeled Alanines” Methods for Transmembrane Helix Alignment
- Tyrosine Replacing Tryptophan as an Anchor in GWALP Peptides
- On the Combined Analysis of 2H and 15N/1H Solid-State NMR Data for Determination of Transmembrane Peptide Orientation and Dynamics
- Single Tryptophan and Tyrosine Comparisons in the N-Terminal and C-Terminal Interface Regions of Transmembrane GWALP Peptides
- Control of Transmembrane Helix Dynamics by Interfacial Tryptophan Residues
Showing 5 of 7 shared publications
- Helix formation and stability in membranes
- Control of Transmembrane Helix Dynamics by Interfacial Tryptophan Residues
- Transmembrane Helix Integrity versus Fraying To Expose Hydrogen Bonds at a Membrane–Water Interface
- Breaking the Backbone: Central Arginine Residues Induce Membrane Exit and Helix Distortions within a Dynamic Membrane Peptide
- Influence of Lipid Saturation, Hydrophobic Length and Cholesterol on Double‐Arginine‐Containing Helical Peptides in Bilayer Membranes
Showing 5 of 7 shared publications
- Helix formation and stability in membranes
- Transmembrane Helix Integrity versus Fraying To Expose Hydrogen Bonds at a Membrane–Water Interface
- Influence of Lipid Saturation, Hydrophobic Length and Cholesterol on Double‐Arginine‐Containing Helical Peptides in Bilayer Membranes
- Influence of interfacial tryptophan residues on an arginine-flanked transmembrane helix
- Examination of pH dependency and orientation differences of membrane spanning alpha helices carrying a single or pair of buried histidine residues
Showing 5 of 7 shared publications
- Comparison of “Polarization Inversion with Spin Exchange at Magic Angle” and “Geometric Analysis of Labeled Alanines” Methods for Transmembrane Helix Alignment
- Tyrosine Replacing Tryptophan as an Anchor in GWALP Peptides
- On the Combined Analysis of 2H and 15N/1H Solid-State NMR Data for Determination of Transmembrane Peptide Orientation and Dynamics
- Single Tryptophan and Tyrosine Comparisons in the N-Terminal and C-Terminal Interface Regions of Transmembrane GWALP Peptides
- Proline Kink Angle Distributions for GWALP23 in Lipid Bilayers of Different Thicknesses
Showing 5 of 6 shared publications
- Ionization Properties of Histidine Residues in the Lipid Bilayer Membrane Environment
- Dynamic regulation of lipid–protein interactions
- Control of Transmembrane Helix Dynamics by Interfacial Tryptophan Residues
- Influence of High pH and Cholesterol on Single Arginine-Containing Transmembrane Peptide Helices
- Influence of Lipid Saturation, Hydrophobic Length and Cholesterol on Double‐Arginine‐Containing Helical Peptides in Bilayer Membranes
Showing 5 of 6 shared publications
- Modulation of Gramicidin Channel Structure and Function by the Aliphatic “Spacer” Residues 10, 12, and 14 between the Tryptophans
- Neighboring Aliphatic/Aromatic Side Chain Interactions between Residues 9 and 10 in Gramicidin Channels
- Helix sense of gramicidin channels as a “nonlocal” function of the primary sequence.
- Peptide Backbone Chemistry and Membrane Channel Function: Effects of a Single Amide-to-Ester Replacement on Gramicidin Channel Structure and Function
- Steric Interactions of Valines 1, 5, and 7 in [Valine 5, d-Alanine 8] Gramicidin A Channels
- Buried lysine, but not arginine, titrates and alters transmembrane helix tilt
- Tyrosine Replacing Tryptophan as an Anchor in GWALP Peptides
- Comparisons of Interfacial Phe, Tyr, and Trp Residues as Determinants of Orientation and Dynamics for GWALP Transmembrane Peptides
- Interactions of drugs and amphiphiles with membranes: modulation of lipid bilayer elastic properties by changes in acyl chain unsaturation and protonation
- Single Tryptophan and Tyrosine Comparisons in the N-Terminal and C-Terminal Interface Regions of Transmembrane GWALP Peptides
- Gramicidin Channels
- Gramicidin A Backbone and Side Chain Dynamics Evaluated by Molecular Dynamics Simulations and Nuclear Magnetic Resonance Experiments. I: Molecular Dynamics Simulations
- Gramicidin Channels: Versatile Tools
- Gramicidin A Backbone and Side Chain Dynamics Evaluated by Molecular Dynamics Simulations and Nuclear Magnetic Resonance Experiments. II: Nuclear Magnetic Resonance Experiments
- Different Membrane Anchoring Positions of Tryptophan and Lysine in Synthetic Transmembrane α-Helical Peptides
- Induction of Nonbilayer Structures in Diacylphosphatidylcholine Model Membranes by Transmembrane α-Helical Peptides: Importance of Hydrophobic Mismatch and Proposed Role of Tryptophans
- Influence of Lipid/Peptide Hydrophobic Mismatch on the Thickness of Diacylphosphatidylcholine Bilayers. A 2H NMR and ESR Study Using Designed Transmembrane α-Helical Peptides and Gramicidin A
- Modulation of membrane structure and function by hydrophobic mismatch between proteins and lipids
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