L. C. Wheeler

Structure and contingency determine mutational hotspots for flower color evolution

This study uses computational simulations to show that mutational hotspots in flower color evolution are shaped by pathway structure and historical contingency, with mutation types and order depending on evolutionary context.

Learning Peptide Recognition Rules for a Low-Specificity Protein

The paper trains a machine learning model to predict peptide binding specificity for a low-specificity protein by analyzing biochemical features rather than amino acid sequences, revealing hydrophobicity and shape complementarity as key factors.

Were ancestral proteins less specific?

The study revisits the evolution of peptide binding specificity in S100A5 and S100A6, showing that ancestral proteins have similar specificity to modern ones when measured against random peptides, challenging previous conclusions.

Computational modeling of anthocyanin pathway evolution: Biases, hotspots, and trade-offs

The paper develops a kinetic model of the anthocyanin pathway to study evolutionary trade-offs and mutation patterns in pigment production.

pytc: a python package for analysis of Isothermal Titration Calorimetry experiments

pytc is a Python package for analyzing Isothermal Titration Calorimetry data using global fits of thermodynamic models.

Conservation of specificity in two low-specificity proteins

This study shows that low-specificity S100 proteins maintain conserved peptide binding specificity across species, indicating evolutionary constraints and subfunctionalization of paralogs.