Christopher B. Prior

Carbonara uses SAXS data to predict alternative protein conformations, enabling more accurate MD simulations of solution-state dynamics.

This study identifies MdfA as a ClpC adaptor protein in Bacillus subtilis that promotes spore metabolic dormancy by inducing ClpCP-mediated degradation of metabolic enzymes.

The paper introduces new topological measures for comparing protein structures, identifies common substructures, and provides a tool for calculating these metrics.

This paper introduces an ab-initio method to derive 3D protein structures from SAXS data and primary sequences, validated using crystal structures and showing success in modeling a coiled-coil protein.