Arthur D. Laganowsky

This study investigates how site-specific hydration affects the thermal stability of proteins and protein complexes using D2O and experimental methods, revealing that stabilization depends on both hydration extent and water interaction sites.

This study uses vT-ESI nMS to analyze how temperature-dependent changes in protein and solution dynamics affect ligand-binding thermodynamics in multiligand protein complexes.

The paper determines the structure of PTDSS2 from Equus caballus in complex with PE or serine substrates, revealing substrate binding sites and PLD activity.

This study investigates how Zn2+ activates PaMsbA, an ABC transporter in Pseudomonas aeruginosa, by enhancing its ATPase activity and promoting dimerization.

This study investigates how vertebrate hemoglobin evolved from a homodimeric ancestor to a heterotetramer through simple genetic changes that exploited symmetry in its structure.

This study uses native mass spectrometry to investigate how different detergents and charge-reducing molecules affect protein-lipid interactions in membrane proteins.

The paper determines the structures of Cry11Aa and Cry11Ba toxins using serial femtosecond crystallography, revealing new insights into their in vivo crystallization patterns and toxicity.