Ahhyun Son

Ahhyun Son serves as a Research Assistant Professor in the Department of Chemistry & Biochemistry within the College of Natural Sciences and Mathematics at the University of Denver. Her research focuses on biochemical mechanisms of protein stability and folding, with particular emphasis on nucleic acid structures in cellular proteostasis.

Dr. Son's primary research interests center on G-quadruplex-mediated chaperone activity, protein aggregation prevention, and the development of intein-based biosensors for in vivo stability monitoring. Her work bridges molecular biology and therapeutic biochemistry, investigating how RNA/DNA structures function as sequence-dependent chaperones to combat neurodegenerative protein misfolding. Current projects explore chapernas (RNA-dependent chaperones) and foldamer therapeutics targeting α-synuclein pathways.

Analysis of her 2019-2025 publications reveals an evolutionary trajectory from influenza virology toward fundamental proteostasis mechanisms. Her most impactful work demonstrates G-quadruplexes' capacity to rescue protein folding and prevent aggregation, with recent studies (2023-2025) focusing on biosensor development and therapeutic applications for protein misfolding diseases.

Scientific Awards:

• No awards explicitly documented in source materials

While specific student mentorship records are absent, Dr. Son's prolific publication output (15+ articles since 2019) suggests active supervision of graduate researchers and substantial grant funding, likely from NIH or NSF programs supporting protein biochemistry and nucleic acid therapeutics. Her research group appears focused on translating basic proteostasis mechanisms into biomedical applications.

Dr. Son's laboratory operates within DU's Chemistry & Biochemistry infrastructure, employing interdisciplinary approaches that integrate biophysical assays, cell-based models, and structural analysis. Collaborative networks with virology and neuroscience teams appear integral to her investigation of protein-nucleic acid interactions in disease contexts.