772305 Practical course in biochemistry II
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- Exercise course
- Semester hours
- Lecturer (assistant)
- Offered in
- Sommersemester 2020
- Languages of instruction
Criteria of protein purity and protein stability
Circular dichroism and Fluorescence-spectroscopy in the study of proteins
Computer analysis of protein structure
Steady-state and presteady-state kinetic analysis
Mass spectrometric methods
- Previous knowledge expected
Bachelors degree; fundamental biochemical knowledge; fundamental practical experience
- Objective (expected results of study and acquired competences)
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.
You can find more details like the schedule or information about exams on the course-page in BOKUonline.