Paola Laurino

This study shows that enzymes in biomolecular condensates enhance catalytic activity through crowding-induced conformational changes and enable increased mobility despite environmental viscosity.

This paper introduces LagTag, a method to recover both earlier and endpoint chromatin states in mammalian cells, and applies it to study dynamic chromatin transitions during stem cell differentiation.

The paper shows that a spontaneous post-translational succinimide modification in a bacterial solute-binding protein enhances its thermostability and binding affinity for 5-oxoproline.

The paper identifies a triple-deletion mutant of SRC kinase that alters activation loop dynamics, leading to changes in substrate preference and signaling outcomes.

The paper reveals how thermodynamic principles shape the biophysical properties of proteins through allosteric regulation and evolutionary tradeoffs.

This study engineers Oxalate decarboxylase to improve its activity and stability for medical applications in hyperoxaluria treatment.

This paper challenges the evolutionary model that the Walker A motif was a seed for early P-loop NTPases by showing that disembodied Walker A peptides do not form stable phosphate-binding nests.

This study shows enzymatic activity reduces viscosity in crowded environments, enhancing substrate diffusion by up to three-fold through disruption of non-covalent interactions.

The paper identifies residue inversions in protein phylogenies to uncover functional divergence after gene duplication, finding 19 such sites in EGFR sequences across 88 fish species.

This study shows that single-mutant EGF ligands alter EGFR dimer stability and signaling, supporting biased signaling theory.