Martin McCullagh

This paper investigates how the L405D mutation in SARS-CoV-2 nsp13 decouples ATP hydrolysis from RNA translocation by altering conformational dynamics.

This study investigates how glycosylation affects the conformational behavior of sarcoglycans and their heterotrimer, revealing structural changes that impact complex stability and muscular dystrophy.

This study reveals ATP-dependent coupling between nucleotide and RNA affinity in WNV NS3h, showing how motif VIL residues modulate RNA binding through conformational changes.

This paper provides a tutorial on using ShapeGMM to cluster and sample biomolecular conformations from molecular dynamics simulations.

The paper improves collective variables for biased sampling by iteratively refining them using enhanced sampling data and a probabilistic clustering model.

This study identifies the motif-VI loop as a nucleotide valve in the West Nile Virus NS3 helicase, showing its role in ATP hydrolysis and viral replication through molecular simulations and experimental validation.

This paper introduces frame-weighted shapeGMM to quantify unbiased biomolecular conformational ensembles from biased simulations, showing improved accuracy in thermodynamic property calculations and structural transitions.

This paper investigates the ATP hydrolysis and product release mechanism of SARS-CoV-2 NSP13 using molecular dynamics simulations and identifies key residues involved in RNA translocation.