The identification and characterisation of proteins and protein complexes is central to the work carried out in my laboratory. Heading up the University of Leicester Proteomics Facility my group uses cutting-edge analytical technologies in pursuing these goals. Our laboratory is equipped with a number of mass spectrometers including LTQ-Orbitrap-Velos (with ETD) and 4000 Q-Trap.Protein phosphorylation site analysis is an area of increasing speciality within the Proteomics group, underpinning much of the research carried out by the many Cell Signalling groups at the University of Leicester. Strategies typically involve chromatographic separation using HILIC, ERLIC or Cation Exchange follwed by phosphopeptide enrichment using IMAC or TiO2. The raw power of the LTQ-Orbitrap is utilised for phospho site discovery and the specfic scan features of the 4000 Q-Trap are harnessed for validation.Together with many colleagues across the 'College of Medicine, Biological Sciences and Psychology', I am currently working on a diverse range of proteomics projects. Key amongst these are:- Quantification of the Plasmodium falciparum phosphoproteome during red blood cell invasion.- The role of phosphorylation in the regulation of memory and learning.- Control of gene expression by alternative splicing.- Study of the 26S proteasome.- Regulation of Mycobacterium tuberculosis metabolism by serine/threonine protein kinases.In addition I have long-standing collaborations with groups at Imperial College London, the University of Sheffield and Radboud University Nijmegen (the Netherlands).Subtle changes in protein expression are increasingly key in many of these studies. Quantitative proteomic approaches, both labelled (Silac and iTRAQ) and label-free (SRM and Spectral Counting), are being utilised to elucidate these changes.