Abstract
Proteins evolve through sequence changes that shape structure, stability,
and function. Ancestral sequence reconstruction (ASR) infers ancestral
proteins from modern homologs, but many studies focus on sequence
inference without evaluating structural or energetic feasibility.
β-lactamases provide an ideal model due to their evolutionary diversity and
clinical relevance in antibiotic resistance.
Here, we present an integrated ASR workflow combining phylogenetic
inference (IQ-TREE), ancestral reconstruction, and structural and stability
validation using AlphaFold and FoldX. By reanalyzing a curated β-
lactamase dataset and comparing with a recent study (Risso et al., 2013),
we provide a controlled comparison of ancestral sequences, predicted
structures, and thermodynamic stability.
Faculty Advisor
Masakatsu Watanabe
Department/Program
Chemistry
Submission Type
in-person poster
Date
4-13-2026
Rights
Copyright the Author(s)
Recommended Citation
Park, Jeyun and Watanabe, Masakatsu
(2026)
"Exploring Ancestral Enzymes through Sequence Reconstruction and Stability Prediction,"
SACAD: Scholarly Activities: Vol. 2026, Article 67.
Available at:
https://scholars.fhsu.edu/sacad/vol2026/iss2026/67
