Stephanie A. M. Wankowicz

WaterFlow predicts ordered water molecule positions in protein structures with sub-angstrom accuracy, outperforming existing methods and improving drug design and crystallographic refinement.

The paper predicts binding entropy using crystallographic ensembles and shows a strong correlation with experimental measurements across multiple protein-ligand pairs.

The paper uses crystallographic ensembles to quantify conformational entropy changes in SARS-CoV-2 Macrodomain upon ligand binding, linking structural heterogeneity to binding thermodynamics.

The paper improves qFit-ligand to better model ligand conformations in structural data, enhancing analysis of conformational heterogeneity in ligand-bound structures.

The paper identifies that small molecule binding sites in PDB structural models are more accurately modeled than other regions, affecting structural interpretation and applications.

Affinity-purification mass spectrometry of 26 SARS-CoV-2 proteins in HEK293T cells yields 332 high-confidence host interactions and 67 druggable human proteins with known compounds.