C. R. Pudney

Cooperative conformational transitions and the temperature dependence of enzyme catalysis

This study investigates the temperature dependence of enzyme catalysis by analyzing MalL and its mutants, showing cooperative conformational transitions and introducing models to explain non-Arrhenius behavior.

N-linked glycosylation increases horse radish peroxidase rigidity leading to enhanced activity and stability.

This study shows glycosylation increases the rigidity of horseradish peroxidase, enhancing its activity and stability through structural changes.

A thermodynamic model for interpreting tryptophan excitation-energy-dependent fluorescence spectra provides insight into protein conformational sampling and stability

The paper develops a thermodynamic model to quantify the relationship between the tryptophan red edge excitation shift effect and protein flexibility, using examples across multiple scales and protein types.

Chemical mapping exposes the importance of active site interactions in governing the temperature dependence of enzyme turnover

The paper maps how substrate interactions affect enzyme temperature dependence and global protein dynamics using a promiscuous enzyme.

Reliable in silico ranking of engineered therapeutic TCR binding affinities with MMPBSA and MMGBSA.

This study develops protocols for reliable in silico ranking of TCR binding affinities using MMPBSA and MMGBSA methods, showing that short MD simulations can accurately evaluate TCR variants.

Rigidifying a de novo enzyme increases activity and induces a negative activation heat capacity

This study shows that increasing rigidity in a de novo peroxidase enhances its activity but alters its temperature dependence, resembling natural enzymes.

Structure and dynamics of a cold-active esterase reveals water entropy and active site accessibility as the likely drivers for cold-adaptation

This study determines the structure of a cold-active esterase and identifies increased substrate accessibility and water entropy tolerance as the main drivers of its cold adaptation.

Monoclonal antibody stability can be usefully monitored using the excitation-energy-dependent fluorescence edge-shift

This paper demonstrates that quantifying the fluorescence red edge excitation shift (REES) can sensitively monitor monoclonal antibody stability across timeframes and concentrations.

Conformation control of the histidine kinase BceS of Bacillus subtilis by its cognate ABC-transporter facilitates need-based activation of antibiotic resistance

The paper shows how the histidine kinase BceS of Bacillus subtilis is controlled by its cognate ABC-transporter to enable energy-efficient antibiotic resistance activation based on need.