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  2024 April 30th, May 2nd, 3rd, 7th, 8th, 9th, 13th, 14th

Schedule 10 sessions (lectures and practical workshops) 

Module coordinator  Prof. Matthias Wilm

Venue  Onsite - April 30th, May 2nd - UCD Conway Institute Seminar Room 2 (G028)
                          May 3rd  - UCD Conway Institute Seminar Room 1 (G027)
                          May 7th, 8th, 9th, 13th, 14th - UCD Conway Institute Seminar Room 1 (G027)

Registration Closes: 23rd April 2024

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