Bi7050 Protein characterisation using mass spectrometry

Faculty of Science
Autumn 2008
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).
Teacher(s)
prof. RNDr. Zbyněk Zdráhal, Dr. (lecturer)
RNDr. Hana Konečná (lecturer)
prof. RNDr. Šárka Pospíšilová, Ph.D. (lecturer)
Guaranteed by
prof. RNDr. Jiří Fajkus, CSc.
Department of Experimental Biology – Biology Section – Faculty of Science
Contact Person: prof. RNDr. Zbyněk Zdráhal, Dr.
Timetable
Fri 10:00–11:50 Kontaktujte učitele
Prerequisites
Basic knowledge of biochemistry and molecular biology
Course Enrolment Limitations
The course is also offered to the students of the fields other than those the course is directly associated with.
fields of study / plans the course is directly associated with
there are 26 fields of study the course is directly associated with, display
Course objectives
Lecture, directed mainly to students of biological programs, gives a brief introduction into mass spectrometry (MS) of proteins including selected related techniques and examples of MS applications. The main goal of the lecture is understanding of principles and possibilities of mass spectrometry in protein characterization. Student should obtain an overview of MS applicability in molecular biological and medical research and other fields.
Syllabus
  • 1. Mass spectrometry (MS)
  • Method principles, method possibilities, 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. Strategies for processing of protein samples (selection of appropriate techniques in consideration of purpose of experiment).
  • 3. Basic methods of protein identification
  • Peptide mapping, MS/MS ion search, identification of proteins with unknown sequence(de-novo sequencing), basic proteomic approaches (bottom-up, top-down), protein homology.
  • 4. Quantification
  • Methods of relative and absolute quantification in mass spectrometry (mass labels, isobaric labels-iTRAQ).
  • 5. Determination of protein modifications
  • Overview of modification types (chemical, post-translational modifications), mutations. Phosphoproteins - sample preparation and detection, localization of phosphorylations. Glycoproteins sample preparation and detection, glycan analysis.
  • 6. Protein arrays (RNDr. Šárka Pospíšilová, PhD)
  • Protein array types, their preparation, detection a quantification.
  • 7. Proteomic applications
  • Mass spectrometry and disease diagnostics (biomarker identification, protein profiling), proteomic projects in our Core lab.
Literature
  • Proteome research : mass spectrometry. Edited by Peter James. Berlin: Springer-Verlag, 2001, xxi, 274 s. ISBN 3-540-67255-9-. info
Assessment methods
lecture, colloquium
Language of instruction
Czech
Further comments (probably available only in Czech)
Study Materials
The course is taught annually.
The course is also listed under the following terms Autumn 2007 - for the purpose of the accreditation, Autumn 2010 - only for the accreditation, Autumn 2005, Autumn 2006, Autumn 2007, Autumn 2009, Autumn 2010, Autumn 2011, Autumn 2011 - acreditation, Autumn 2012.
  • Enrolment Statistics (Autumn 2008, recent)
  • Permalink: https://is.muni.cz/course/sci/autumn2008/Bi7050