Proteins & Proteomics

Held at University of Glasgow, Co-ordinated by Dr Richard Burchmore

Part 1

Taught lectures:

  • The genome, transcriptome, proteome and metabolome – cell structure, function and organisation
  • Basic molecular biology, PCR, cloning, protein expression, cell culture
  • Protein biophysical properties and structure
  • Chromatography: theory of ion-exchange, reversed phase, size exclusion, affinity chromatography, etc. Surface chemistry and mixed binding modes.
  • High performance liquid chromatography (HPLC), multidimensional liquid chromatography (MDLC), complex solvent systems.
  • Capillary electrophoresis (CE, CEC, FFE)
  • Polyacrylamide gel electrophoresis

Practical training:

  • Sample preparation: growth of cells and isolation of biomolecules (protein, RNA)
  • Protein enrichment. Protein assay. RNA assay and QC.
  • Protein separation: 1D-PAGE, RP-LC, SAX, size exclusion, or CE.
  • Samples retained for proteomics and genomics course.

Part 2

Taught lectures:

  • Proteomics – methodologies and workflows
  • Underlying principles and challenges
  • Protein fractionation and enrichment methods including modern affinity enrichment methods and protein complex capture
  • Advanced chromatography and mass spectrometry
  • Quantitative methodologies- ICAT, iTRAQ, DiGE, others
  • Introduction to bioinformatics
  • Protein immobilisation chemistries and protein arrays
  • Metabolomics – methodologies and workflows
  • Basic principles – small molecule separation, measurement and analysis (MS, NMR)
  • Metabolic networks, control, exploitation

Practical training:

  • 2D-minigel
  • Spot picking and sample preparation
  • MALDI-ToF and ToF-ToF, LC-ESI-MSMS