TSD203

Elective Course, Basic proteomics principles, techniques and application areas

Faculty \ Department
School of Medicine \ Medicine
Course Credit
ECTS Credit
Course Type
Instructional Language
3
3
Elective
Turkish
Prerequisites
-
Programs that can take the course
Licence
Course Description

The backbone of proteomics is formed by two-dimensional gel electrophoresis and mass spectrometry. In this course, an introduction will be made by discussing the basic structure and properties of proteins, -omics technologies and proteomics concepts will be explained, how to obtain and quantify proteins from various cells and tissues, one-dimensional (SDS-PAGE) and two-dimensional (2D PAGE) gel electrophoresis, how they are analyzed and what kind of information they provide, protein identification with mass spectrometry and advanced bioinformatics analyses will be taught. The Western Blot method, which we use in the determination of a specific protein, will also be explained in this course, and its connections with previously explained topics will be established and reinforced.
Textbook and / or References
1. Temel Proteomik Stratejiler, Özel Duygu Demiralp, İğci Naşit, Peker
Selen, Ayhan Beycan, 2014, Ankara Üniversitesi Yayınevi, ISBN: 978-605-136-148-2, 2014
ntroduction to Proteomics: Principles and Applications. Nawin C. Mishra, Günter Blobel, 2010.
2. Molecular Genetics and Personalized Medicine. D. Hunter Best ? Jeffrey J. Swensen Eds. Springer Science+Business Media, LLC (2012).
3. Molecular Medicine ?Genomics to Personalized Healthcare?. 4th ed. Ronald J Trent (2012).
4. Proteomics: A Cold Spring Harbor Laboratory Course Manual, Andrew J. Link, Editor: Andrew J. Link
5. Clinical Proteomics: From Diagnosis to Therapy
İlk Yayınlanma Tarihi: 2008
Jennifer E. Van Eyk (Editor), Michael J. Dunn (Editor)
Course Objectives
With the completion of the Human Genome Project, it was seen that genetic information alone would not be sufficient, and in this context, the field of "proteomics" was born by focusing on studies on proteins, which are functional products of genes. The reason for this is that proteins provide more precise information about the dynamic state of the cell, tissue or organism. The majority of the area of ​​use of proteomics methods is in medicine, also called "clinical proteomics", and most of the studies in the field of clinical proteomics are studies on the identification of new biomarkers specific to diseases. Apart from this, proteomics methods are used in many different areas, from target drug development to toxicology and the food industry. The aim of this course is to provide students with information about proteins and basic proteomics technologies, and to teach them in which areas and how they can benefit from these technologies and applications in the clinic.
Course Outcomes
1. Know the basic structure and functions of proteins
2. Knows the concept of Omic technology and Proteomics.
3. Know the basic proteomic study steps.
4. Know about protein purification and protein chromatography techniques and their areas of use.
5. Has knowledge of which protein isolation technique to use for which tissue
6. Learn how to determine protein amount and the various methods used for determination.
7. Knows the proteomic analysis methods and can predict which analysis should be preferred under which conditions.
8. Know the purposes of using SDS-PAGE and 2D-PAGE techniques.
9. Learn how to analyze SDS-PAGE and 2D-PAGE gels.
10. Learn the methods to detect protein changes between groups by performing comparative proteomic analysis under different conditions such as healthy individuals, individuals receiving treatment and patients.
11. Learn how to identify protein biomarker candidates for a disease of interest.
12. Know the types of mass spectrometers and their purposes of use.
13. Knows how to use data obtained from mass spectrometry and bioinformatics analysis.
14. Learn the term blotting and gain an idea about various blotting techniques.
15. Learn the purposes of using the Western blot technique.
16. Learn how to use the Western blot technique in the clinic.
17. Know how to analyze Western blot results.
Tentative Course Plan
Week 1: Protein Basic Structure and Functions
Week 2: -Omic Technologies, Introduction to Proteomics
Week 3: General Strategies in Proteomics
Week 4: Protein Purification; Protein Chromatography
Week 5: Protein Extraction (isolation, extraction)
Week 6: Protein Quantification Methods
Week 7: One-Dimensional Gel Electrophoresis Applications (SDS-PAGE)
Week 8: Two-Dimensional Gel Electrophoresis Applications (2D-PAGE)
Week 9: Analysis of Protein Profile Maps
Week 10: Introduction to Mass Spectrometry Systems and Mass Spectrometry Analyses
Week 11: Bioinformatic Analysis of Mass Spectrometry Data and Protein Identification (MASCOT-MATRIX SCIENCE)
Week 12: Western Blot Technique and Application Areas
Tentative Assesment Methods
• Final exam: 100 %
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