Denise V. Greathouse
Affiliation confirmed via AI analysis of OpenAlex, ORCID, and web sources.
Research Assoc. Professor
Also affiliated: Centre National de la Recherche Scientifique (2000); Université Libre de Bruxelles (2001); University of Miami (2005); Utrecht University (1996–2003); Cornell University (1997–2003); University of Arkansas System (2007); University of Oxford (2003–2010); Max Planck Institute for Biophysical Chemistry (1998); Centre de recherche Paul Pascal (2000); Weill Cornell Medicine (2000–2003); Umeå University (1996); Leipzig University (1998)
Research Areas
Biomedical Subjects
Links
Biography and Research Information
OverviewAI-generated summary
Denise V. Greathouse is a Research Associate Professor at the University of Arkansas at Fayetteville. Her research focuses on the behavior and structure of lipid membranes and their interactions with peptides and proteins. Greathouse has published work investigating how specific amino acid residues, such as glutamic acid and tryptophan, influence membrane properties and protein structure within these environments. Her investigations often employ molecular modeling to understand these complex interactions. She has co-authored publications with researchers including Roger E. Koeppe from the University of Arkansas at Fayetteville and Jake R. Price from the University of Arkansas for Medical Sciences.
With a career marked by significant scholarly output, Greathouse has authored 149 publications, accumulating over 3,900 citations. Her work has been recognized with a designation as a highly cited researcher. Her recent publications in 2021 explored lipid-dependent titration at membrane interfaces and disorder induced by specific amino acids in transmembrane helices.
Metrics
- h-index: 33
- Publications: 150
- Citations: 4,025
Positions
-
Research Assoc. Professor 1988–presentUniversity of Arkansas Fayetteville Chemistry and Biochemistry ORCID
Selected Publications
-
Illuminating Disorder Induced by Glu in a Stable Arg-Anchored Transmembrane Helix (2021)
-
Lipid-Dependent Titration of Glutamic Acid at a Bilayer Membrane Interface (2021)
-
Examination of pH dependency and orientation differences of membrane spanning alpha helices carrying a single or pair of buried histidine residues (2020)
-
Flanking aromatic residue competition influences transmembrane peptide helix dynamics (2020)
-
Effect of pH and Lipid Composition on Membrane-Spanning Helices with Glutamic Acid Examined by Solid-State Nmr (2020)
-
Effect of Charged Lipids on the Ionization Behavior of Glutamic Acid-Containing Transmembrane Helices (2020)
-
Influence of interfacial tryptophan residues on an arginine-flanked transmembrane helix (2019)
-
Lipid Optimization to Improve the Solid-State NMR Spectra from Membrane-Spanning Helices with Glutamic Acid (2019)
-
Breaking the Backbone: Central Arginine Residues Induce Membrane Exit and Helix Distortions within a Dynamic Membrane Peptide (2019)
-
Influence of Lipid Saturation, Hydrophobic Length and Cholesterol on Double‐Arginine‐Containing Helical Peptides in Bilayer Membranes (2019)
-
Position Dependent Orientation Difference of Transmembrane Peptides Flanked by Single or Multiple Histidine Residues (2019)
-
Novel F13,F15 Gramicidin Subunits Predicted to Cross Bilayer Membranes and form Ion Channels (2019)
-
Characterization of Alpha-Helix Distortions at a Membrane Surface and a Partial 3(10)-Helix by Solid-State NMR (2019)
-
Influence of Charged Lipids on Glutamic Acid Containing Transmembrane Helices (2019)
-
Helix Fraying and Orientation of a Transmembrane Peptide having a Long Hydrophobic Core and Anchored by Interfacial Arginine Residues (2019)
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 102 shared publications
- Regulation of Sodium Channel Function by Bilayer Elasticity
- The Preference of Tryptophan for Membrane Interfaces
- Hydrophobic Coupling of Lipid Bilayer Energetics to Channel Function
- Importance of Tryptophan Dipoles for Protein Function: 5-Fluorination of Tryptophans in Gramicidin A Channels
- [28] Design and characterization of gramicidin channels
Showing 5 of 24 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 18 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 17 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
- Tyrosine Replacing Tryptophan as an Anchor in GWALP Peptides
- Influence of Proline upon the Folding and Geometry of the WALP19 Transmembrane Peptide
Showing 5 of 13 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 13 shared publications
- Dynamic regulation of lipid–protein interactions
- Juxta‐terminal Helix Unwinding as a Stabilizing Factor to Modulate the Dynamics of Transmembrane Helices
- Influence of glutamic acid residues and pH on the properties of transmembrane helices
- Influence of pH and Side-Chain Negative Charge on the Behavior of Designed Transmembrane Peptides in Lipid Bilayers
- Influence of Glutamic Acid Residues on the Properties of Model Membrane-Spanning Helices
Showing 5 of 12 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
- [28] Design and characterization of gramicidin channels
- 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 10 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
- Orientations of the tryptophan 9 and 11 side chains of the gramicidin channel based on deuterium nuclear magnetic resonance spectroscopy
- Interfacial Positioning and Stability of Transmembrane Peptides in Lipid Bilayers Studied by Combining Hydrogen/Deuterium Exchange and Mass Spectrometry
Showing 5 of 9 shared publications
- Tyrosine Replacing Tryptophan as an Anchor in GWALP Peptides
- 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
- Proline Kink Angle Distributions for GWALP23 in Lipid Bilayers of Different Thicknesses
- Properties of Membrane-Incorporated WALP Peptides That Are Anchored on Only One End
Showing 5 of 7 shared publications
- 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
- Single Tryptophan and Tyrosine Comparisons in the N-Terminal and C-Terminal Interface Regions of Transmembrane GWALP Peptides
- Importance of Aromatic Anchor Residue Identity and Location for the Tilt and Dynamics of Transmembrane Peptides
Showing 5 of 7 shared publications
- [28] Design and characterization of gramicidin channels
- The Structure, Cation Binding, Transport, and Conductance of Gly15-Gramicidin A Incorporated into SDS Micelles and PC/PG Vesicles,
- Design and Characterization of Gramicidin Channels with Side Chain or Backbone Mutations
- Peptide Backbone Chemistry and Membrane Channel Function: Effects of a Single Amide-to-Ester Replacement on Gramicidin Channel Structure and Function
- ChemInform Abstract: Design and Characterization of Gramicidin Channels
- 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
- Combined Experimental/Theoretical Refinement of Indole Ring Geometry Using Deuterium Magnetic Resonance and ab Initio Calculations
- Optimized aminolysis conditions for cleavage of N‐protected hydrophobic peptides from solid‐phase resins
- Peptide Influences on Lipids
- 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
- Tyrosine Replacing Tryptophan as an Anchor in GWALP Peptides
- 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
- Properties of Membrane-Incorporated WALP Peptides That Are Anchored on Only One End
- A Proline Kink in GWALP23
Similar Researchers
Based on overlapping research topics