Simon J. Sharpe

This study identifies domain 36 of tropoelastin as the site of transient interaction with heparin, which nucleates and promotes coacervation through multivalent binding.

The paper introduces FELS, a method to screen free energy landscapes for disordered proteins, and applies it to tropoelastin, revealing its conformational ensemble and resolving conflicting models.

This study shows that an SARS-CoV-2 envelope peptide promotes serum amyloid A misfolding and fibrillization, contributing to amyloid-related complications in hyper-inflammatory conditions.