PřF:S5017 MS in Proteomics - Course Information

S5017 Mass Spectrometry in Proteomics

Extent and Intensity

1/0/0. 1 credit(s) (plus extra credits for completion). Recommended Type of Completion: k (colloquium). Other types of completion: zk (examination).
In-person direct teaching

Teacher(s)

Mgr. Gabriela Lochmanová, Ph.D. (lecturer)
prof. RNDr. Zbyněk Zdráhal, Dr. (lecturer)

Guaranteed by

prof. RNDr. Zbyněk Zdráhal, Dr.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: RNDr. Michaela Fajkusová
Supplier department: Central European Institute of Technology

Prerequisites

Basic knowledge of biochemistry and molecular biology

Course Enrolment Limitations

The course is offered to students of any study field.

Course objectives

The aim of this course is to introduce to students present possibilities of mass spectrometry in proteomics, the basic principles of mass spectrometry, types of MS instrumentation, basics of interpretation of MS and MS/MS data and using examples to present application of appropriate mass spectometric techniques for different types of biological and biomedical experiments.

Learning outcomes

At the end of the course students should be able to: understand and explain the basic principles of mass spectrometry; describe MS instrumentation currently used in proteomics; understand basics of interpretation of MS and MS/MS data; explain principles of protein identification and their posttranslational modifications by mass spektrometry; explain principles of MS quantification methods; describe present possibilities of mass spectrometry in proteomics, propose application of appropriate mass spectrometric techniques for different types of biological and biomedical experiments.

Syllabus

• 1. Mass spectrometry (MS) Method principles, method possibilities in proteomics, overview of MS instrumentation and ionization techniques (MALDI-MS, ESI-IT MS, FTMS, hybrid systems).
• 2. Sample preparation and separation (RNDr. Hana Konečná) General rules for sample preparation before MS analysis. Basic techniques for protein isolation. Overview of separation techniques (electromigration and chromatographic techniques).
• 3. Sample preparation and separation II (Dr. Gabriela Lochmanová) Strategies for processing of protein samples (selection of appropriate techniques in consideration of purpose of experiment).
• 4. Basic methods of protein identification Proteomic approaches (bottom-up, top-down,)peptide mapping, MS/MS ion search, identification of proteins with unknown sequence(de-novo sequencing), protein homology.
• 5. Protein quantification Methods of relative and absolute quantification in mass spectrometry (mass labels, isobaric labels-iTRAQ, TMT, label-free approach).
• 6. Characterization of protein modifications Overview of modification types (chemical, posttranslational modifications), mutations. Phosphoproteins - sample preparation and detection, localization of phosphorylations. Glycoproteins sample preparation and detection, glycan analysis.
• 7. Proteomic applications Mass spectrometry and disease diagnostics (biomarker identification, protein profiling), proteomic projects in our proteomic facility.

Literature

• Proteome research : mass spectrometry. Edited by Peter James. Berlin: Springer-Verlag, 2001, xxi, 274 s. ISBN 3-540-67255-9-. info

Teaching methods

lecture, class discussion

Assessment methods

colloquium or oral examination¨
colloquium: three questions for each student, correct answers to all questions are needed to pass
oral examination: questions and discussion, correct answers to questions (at least 60%) and understanding discussed topics is needed to pass the exam

Language of instruction

English

Further comments (probably available only in Czech)

The course is taught annually.
The course is taught: in blocks.
Note related to how often the course is taught: Two-hour blocks.
Information on the extent and intensity of the course: Two-hour blocks.

• Enrolment Statistics (recent)
  
• Permalink: https://is.muni.cz/course/sci/spring2025/S5017