E. P. O'Brien

A Newly Identified Class of Protein Misfolding in All-atom Folding Simulations Consistent with Limited Proteolysis Mass Spectrometry

The paper identifies entangled misfolded states in all-atom protein folding simulations that resemble native states and are consistent with mass spectrometry data.

Synonymous mutations can alter protein dimerization through localized interface misfolding involving self-entanglements

This paper shows synonymous mutations can alter protein dimerization by causing misfolded self-entangled states that disrupt dimer interfaces, with effects dependent on translation speed.

Subpopulations of soluble, misfolded proteins commonly bypass chaperones: How it happens at the molecular level

The paper shows that some soluble, misfolded proteins evade chaperones by being structurally similar to native states, leading to long-term misfolding.

Universal protein misfolding intermediates can bypass the proteostasis network and remain soluble and less-functional

The paper shows that misfolded proteins can bypass proteostasis by being structurally similar to native states and persisting for long periods.

How synonymous mutations alter enzyme structure andfunction over long time scales

This paper shows that synonymous mutations alter enzyme function over time by causing misfolded, entangled protein states that reduce catalytic activity.

Ribosome elongation kinetics of consecutively charged residues are coupled to electrostatic force

The paper shows charged residues affect ribosome elongation speed through mechanochemical forces, supported by simulations and experimental data.

Combinations of slow translating codon clusters can increase mRNA half-life

The paper shows that two slow codon clusters can increase mRNA half-life by suppressing ribosome queues, contrasting the effect of a single cluster.

Domain topology, stability, and translation speed determine mechanical force generation on the ribosome

This study shows that mechanical forces on ribosomes during translation depend on domain stability, topology, and translation speed, with implications for protein structure and evolution.