UCD Conway Institute of Biomolecular and Biomedical Research Institiúid Mhic Con Mí an Taighde Bhithmhóilínigh agus Bhithleighis

CNWY40160 Applied Proteomics

About the course

Designed for students who wish to understand and become critically aware of principles, practice and applications of the rapidly developing proteomic technologies.

Credits ECTS 5

Dates  TBC

Schedule 10 sessions (lectures and practical workshops) 

Module coordinator  Prof. Matthias Wilm

Venue  Onsite - UCD Conway Institute 

Registration Closes: TBC

Places available  20 maximum - limited to the number of spaces available for the practical sessions

Course structure

The module will be delivered in 10 stand-alone blocks, each one composed of 3hr seminar-style sessions (mornings) and 3hr practical sessions (afternoons)

Credit requirements

Mid-course & end course evaluation session: MCQs + problem-based assessment

What does it cover?

  • Refresher of protein biochemistry
  • Gel-based and gel-free separations
  • Mass spectrometric techniques
  • Post-translational modifications and interactomics
  • Protein arrays technology
  • Proteomic bioinformatics
  • Validation techniques
  • Clinical applications of proteomics

Why enrol?

On completion, you will be able to:

  • Understand protein biochemistry principles and be able to apply them to protein separation and purification
  • Have acquired critical awareness of differences between gel-based and gel-free proteomic approaches and be able to run simple electrophoretic separations
  • Demonstrate understanding of the distinction between resolution, accuracy, sensitivity and throughput of a mass spectrometer
  • Formulate the principles of MALDI and ESI mass spectrometry, demonstrate knowledge of the different mass analyzers and detectors and integrate this knowledge with the application of modern methods in label-assisted and label-free quantitative proteomics
  • Be familiar with the techniques for mass spectrometric analysis of intact proteins, protein complexes and their application in the pharmaceutical industry
  • Know the strengths and how to counteract the pitfalls of a quantitative proteomic analysis
  • Demonstrate knowledge and understanding of the most important post-translational modifications of proteins and of methods for their analysis
  • Be familiar with the different techniques used to study protein-protein interactions.
  • Demonstrate understanding of the theory and practice of mass spectrometry data handling with some of the most common bioinformatic algorithms
  • Demonstrate critical awareness of proteomic validation techniques. In particular, be familiar with SRM (selected reaction monitoring) by triple-quadrupole mass spectrometry
  • Be aware of the most up-to-date global proteomic investigation techniques
  • Be able to judge the strengths and limitations of global proteomic investigations
  • Be able to evaluate and describe the impact of the application of proteomic analyses to relevant biomedical and clinical set-ups
  • Be able to critically assess the difficulties involved in investigating different clinical specimens

Next steps