Content (Syllabus outline)
Methods for the determination of protein amino acid sequences: Edman degradation.
Methods for determination of three-dimensional structures of proteins: The goal is to familiarize students with the basics of experimental methods commonly used in structural biology for determination of three-dimensional structures of proteins and other macromolecules, including an explanation of the advantages and disadvantages of each method: X-ray crystallography (basics of crystallography and x-ray scattering), nuclear magnetic resonance (basics of 1H, 13C, 15N NMR), cryo-electron microscopy, small-angle X-ray scattering
Analysis of data obtained by methods of structural biology and validation of results: model building on the basis of experimental data, with emphasis on the specifics of each experimental technique (crystallographic phase problem, coupling in NMR data, etc.), model optimization, validation of built models using appropriate web servers. Data deposition in public databases (e.g. Protein Data bank).
Basics of proteomic methods. An overview of instruments used for separation and detection (mass spectrometry). Description of experimental techniques for identification, characterization and quantification of proteins/peptides. Overview of the differences between experiment design and data analysis. Use of proteomic tools for the identification of novel biological markers and determination of concentration limits for diagnostic and medical puposes.
Analysis of proteomic data obtained by mass spectrometry and validation of results.
Prerequisites
Prerequisites for admittance to final exam:
Practical examination (colloquium)
- presence at at least 80% of practicals.
Exam:
- practical examination (colloquium),
- seminar presentation.