Vicki H. Wysocki

Vicki H. Wysocki develops and applies mass spectrometry techniques, especially native mass spectrometry and ion mobility, to study the structure and organization of protein complexes without disrupting their natural shapes. Her work focuses on methods like surface-induced dissociation, electron capture dissociation, and capillary electrophoresis to reveal how multi-protein assemblies are built and how their subunits interact, with applications ranging from DNA-repair proteins to viral capsids and lipid-binding membrane proteins. This research supports structural biology by providing complementary data to techniques like cryo-EM and computational modeling (e.g., AlphaFold, Rosetta).

Publication output has fluctuated over the last decade with a peak in 2024, following a generally steady-to-growing pattern before a decline in the most recent two years (2025-2026), though this may partly reflect incomplete recent-year data.

Generated by claude-sonnet-5 from public bibliographic data · Jul 20, 2026