Matthew Brownd
This is a likely match — the affiliation was inferred from OpenAlex, ORCID, and web sources but has not been fully confirmed. Treat with appropriate caution.
Researcher
Also affiliated: John Brown University (2018–2019)
Faculty Researcher
Research Areas
Biomedical Subjects
Biography and Research Information
OverviewAI-generated summary
Matthew Brownd's research focuses on understanding the molecular mechanisms of biological transporters, particularly ATP-binding cassette (ABC) transporters. He investigates their conformational cycles and the role of lipid bilayers and nucleotide binding in their function. His work utilizes computational methods, including molecular dynamics simulations and free-energy perturbation calculations, to explore protein binding affinities and conformational dynamics.
Recent publications from Brownd's group have examined the conformational cycle of a protease-containing ABC transporter in lipid nanodiscs, revealing insights into cargo-protein coupling. Other studies have investigated the dynamics of ABC exporters like PCAT1 and P-glycoprotein, as well as the binding activity within HCN channel subfamilies and the conformational dynamics of intrinsically disordered localization sequences. His collaborators at the University of Arkansas at Fayetteville include Adithya Polasa, Mahmoud Moradi, Mortaza Derakhshani-Molayousefi, and Ahmed Shubbar.
Metrics
- h-index: 1
- Publications: 11
- Citations: 12
Selected Publications
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Deciphering Chemomechanical Couplings in Proteins Using Molecular Dynamics and Enhanced Sampling Techniques (2026)Journal of the Arkansas Academy of Science OpenAlex
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An Investigation of the Conformational Dynamics of ABC Exporter PCAT1 using Microsecond-Level MD Simulations (2026)
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Characterizing the Conformational Dynamics of an Intrinsically Disordered Localization Sequence (2026)
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Predicting Binding Affinities for the Binding Domain of Hyperpolarization-Activated Cyclic Nucleotide-Gated Channel Isoforms Using Free-Energy Perturbation (2026)
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BPS2025 - Exploring lipid-protein interactions and nucleotide binding in multidrug resistance protein 1: Insights from molecular dynamics and free energy perturbation simulations (2025)
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Conformational cycle of a protease-containing ABC transporter in lipid nanodiscs reveals the mechanism of cargo-protein coupling (2024)
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Conformational cycle of a protease-containing ABC transporter in lipid nanodiscs reveals the mechanism of cargo-protein coupling (2024)
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Comparison of cyclic AMP binding activity within HCN channel subfamily using atomistic molecular dynamics simulations of isolated cyclic nucleotide binding domains (2023)
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Using molecular dynamics simulations to characterize the structural/conformational effect of amino acid substitutions at the second position of the intrinsically disordered mitochondrial localization peptide (MLP) (2022)
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Investigation of Cyclic AMP Binding Interactions with Isolated Cyclic Nucleotide Binding Domain of HCN1 Channel using Atomistic Molecular Dynamics Simulations at Microsecond Timescale (2021)
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Novel F13,F15 Gramicidin Subunits Predicted to Cross Bilayer Membranes and form Ion Channels (2019)
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Gramicidin Subunits that Cross Membranes and form Ion Channels (2018)
Collaboration Network
Top Collaborators
- Conformational cycle of a protease-containing ABC transporter in lipid nanodiscs reveals the mechanism of cargo-protein coupling
- Investigation of Cyclic AMP Binding Interactions with Isolated Cyclic Nucleotide Binding Domain of HCN1 Channel using Atomistic Molecular Dynamics Simulations at Microsecond Timescale
- Using molecular dynamics simulations to characterize the structural/conformational effect of amino acid substitutions at the second position of the intrinsically disordered mitochondrial localization peptide (MLP)
- Comparison of cyclic AMP binding activity within HCN channel subfamily using atomistic molecular dynamics simulations of isolated cyclic nucleotide binding domains
- Conformational cycle of a protease-containing ABC transporter in lipid nanodiscs reveals the mechanism of cargo-protein coupling
Showing 5 of 9 shared publications
- Conformational cycle of a protease-containing ABC transporter in lipid nanodiscs reveals the mechanism of cargo-protein coupling
- Investigation of Cyclic AMP Binding Interactions with Isolated Cyclic Nucleotide Binding Domain of HCN1 Channel using Atomistic Molecular Dynamics Simulations at Microsecond Timescale
- Conformational cycle of a protease-containing ABC transporter in lipid nanodiscs reveals the mechanism of cargo-protein coupling
- Conformational cycle of a protease-containing ABC transporter in lipid nanodiscs reveals the mechanism of cargo-protein coupling
- Conformational cycle of a protease-containing ABC transporter in lipid nanodiscs reveals the mechanism of cargo-protein coupling
- Conformational cycle of a protease-containing ABC transporter in lipid nanodiscs reveals the mechanism of cargo-protein coupling
- Conformational cycle of a protease-containing ABC transporter in lipid nanodiscs reveals the mechanism of cargo-protein coupling
- Conformational cycle of a protease-containing ABC transporter in lipid nanodiscs reveals the mechanism of cargo-protein coupling
- Conformational cycle of a protease-containing ABC transporter in lipid nanodiscs reveals the mechanism of cargo-protein coupling
- Conformational cycle of a protease-containing ABC transporter in lipid nanodiscs reveals the mechanism of cargo-protein coupling
- Conformational cycle of a protease-containing ABC transporter in lipid nanodiscs reveals the mechanism of cargo-protein coupling
- Conformational cycle of a protease-containing ABC transporter in lipid nanodiscs reveals the mechanism of cargo-protein coupling
- Conformational cycle of a protease-containing ABC transporter in lipid nanodiscs reveals the mechanism of cargo-protein coupling
- BPS2025 - Exploring lipid-protein interactions and nucleotide binding in multidrug resistance protein 1: Insights from molecular dynamics and free energy perturbation simulations
- BPS2025 - Exploring lipid-protein interactions and nucleotide binding in multidrug resistance protein 1: Insights from molecular dynamics and free energy perturbation simulations
- BPS2025 - Exploring lipid-protein interactions and nucleotide binding in multidrug resistance protein 1: Insights from molecular dynamics and free energy perturbation simulations
- Predicting Binding Affinities for the Binding Domain of Hyperpolarization-Activated Cyclic Nucleotide-Gated Channel Isoforms Using Free-Energy Perturbation
- Predicting Binding Affinities for the Binding Domain of Hyperpolarization-Activated Cyclic Nucleotide-Gated Channel Isoforms Using Free-Energy Perturbation
- Characterizing the Conformational Dynamics of an Intrinsically Disordered Localization Sequence
- Characterizing the Conformational Dynamics of an Intrinsically Disordered Localization Sequence
- An Investigation of the Conformational Dynamics of ABC Exporter PCAT1 using Microsecond-Level MD Simulations
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