772305 Practical course in biochemistry II (in Eng.)

Art
Übung
Semesterstunden
5
Vortragende/r (Mitwirkende/r)
Parzer, Bianca , Falb, Nikolaus , Leitgeb, Urban , Fink, Jasmin , Sumesgutner, Delia , Zajc, Charlotte , Gabler, Thomas , Pfanzagl, Vera , Grünwald-Gruber, Clemens , Hofbauer, Stefan , Furtmüller, Paul Georg , Wilson, Iain B.H. , Staudacher, Erika , Traxlmayr, Michael , Obinger, Christian
Organisation
Angeboten im Semester
Wintersemester 2023/24
Unterrichts-/ Lehrsprachen
Englisch
Lehrinhalt

Chromatographic procedures

Electrophoresis methods

Criteria of protein purity and protein stability

Spectroscopic methods for studying proteins

Thermodynamic of proteins

Steady-state and pre-steady-state kinetic methodes

Mass spectrometric methods.
Inhaltliche Voraussetzungen (erwartete Kenntnisse)

Bachelors degree; fundamental biochemical knowledge; fundamental practical experience
Lehrziel

Aim of the course is the acquirement of different methods for characterizing the structure and function of recombinant proteins and enzymes.

After successful attendance of this course the students should be familiar with the fundamentals of chromatographic methods and their practical application for protein purification. They know methods to evaluate protein purity and protein stability and have the knowledge to apply these methods. The students now know the basics of several spectroscopic methods (UV-vis and fluorescence spectroscopy, CD spectroscopy) and can describe them. After using these methods on selected samples, students should be able to choose the appropriate method for similar samples self-dependent. They are able to analyze (recombinant) proteins with different kinetic models and evaluate the kinetic data. They can describe common mass spectrometric methods used in protein chemistry and have the knowledge to apply these methods on defined samples. The students are able to perform spectroscopic and computer-supported structure analysis and to compare and assess the results.
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