Colin D. Heyes Source Confirmed
Affiliation confirmed via AI analysis of OpenAlex, ORCID, and web sources.
Professor / Department Chair
University of Arkansas at Fayetteville
faculty
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Biography and Research Information
OverviewAI-generated summary
Colin D. Heyes' research focuses on the structure-optics relationships in colloidal quantum dots, with applications in areas such as fluorescence imaging and light-emitting diodes. His work utilizes an integrative approach combining experimental and computational methods, including single-molecule Förster Resonance Energy Transfer (smFRET) and molecular dynamics simulations, to investigate the structural dynamics and photophysical properties of nanomaterials and biomolecules.
His federal grant funding from the National Science Foundation supports investigations into structure-optics property relationships in homogeneous and alloyed colloidal quantum dots. Heyes has published extensively on topics including quantum dot synthesis and characterization, protein structure and dynamics, and the development of advanced imaging techniques. His scholarship metrics include an h-index of 24, with over 2,200 citations across 63 publications. Key collaborators at the University of Arkansas at Fayetteville include Mercede Furr, Thallapuranam Krishnaswamy Suresh Kumar, Vivek Govind Kumar, and Mahmoud Moradi, with whom he has co-authored multiple publications.
Metrics
- h-index: 24
- Publications: 63
- Citations: 2,252
Selected Publications
- All-inorganic QLEDs utilizing resonant energy transfer between non-stoichiometric nickel oxide hole transport layer and alloyed CdSe/ZnS quantum dots (2025) DOI
- cpSRP43 Is Both Highly Flexible and Stable: Structural Insights Using a Combined Experimental and Computational Approach (2023) DOI
- Compact, Fast Blinking Cd-Free Quantum Dots for Super-Resolution Fluorescence Imaging (2023) DOI
- An integrative approach to molecular dynamics and single molecule FRET techniques (2023) DOI
- Transient local secondary structure in the intrinsically disordered C‐term of the Albino3 insertase (2022) DOI
- cpSRP43 is both highly flexible and stable: Structural insights using a combined experimental and computational approach (2022) DOI
- Site-specific labeling and functional efficiencies of human fibroblast growth Factor-1 with a range of fluorescent Dyes in the flexible N-Terminal region and a rigid β-turn region (2021) DOI
- Transient local secondary structure in the intrinsically disordered C-term of the Albino3 insertase (2021) DOI
- Integrating Molecular Dynamics and smFRET Data to Study the Conformational Ensemble of the C-Terminus of Albino3 Protein (2021) DOI
Federal Grants 1 $535,560 total
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