Matthew Brownd Data-verified
Affiliation confirmed via AI analysis of OpenAlex, ORCID, and web sources.
Researcher
faculty
Research Areas
Biography and Research Information
OverviewAI-generated summary
Matthew Brownd's research focuses on understanding the molecular mechanisms of cellular transport and protein function, particularly utilizing computational and biophysical approaches. His work investigates the conformational dynamics and mechanisms of ATP-binding cassette (ABC) transporters, which play crucial roles in cellular processes and disease states. Brownd has published research on the conformational cycle of protease-containing ABC transporters, revealing how they couple cargo-protein transport. His studies also explore the structural and conformational effects of genetic variations and molecular interactions, such as nucleotide binding in ion channels and amino acid substitutions in intrinsically disordered peptides. Brownd has collaborated with researchers at the University of Arkansas at Fayetteville, including Adithya Polasa and Mahmoud Moradi, on multiple publications.
Metrics
- h-index: 1
- Publications: 11
- Citations: 10
Selected Publications
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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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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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