Protein science: Structure, interactions and molecular properties

• Describe and evaluate the chemical structure and properties of the amino acids both alone and in the context of protein structure
• Understand, differentiate and evaluate the different forces and bonding types in proteins.
• Evaluate advantages and limitations of different methods in protein science.
• Design basic studies of the structure, stability, function and interactions of proteins.
• Evaluate measuring principles of crucial methods in protein science, and assess errors and overall certainty.
• Discuss protein structure determinations and their use (X-ray crystallography, cryo-electron microscopy)
• Describe the underlying mechanisms behind protein folding and flexibility and deduce the impact of these on molecular function.
• Explain the underlying mechanisms of protein interactions.
• Understand the analytical process of scientific decision making and prioritisation
• Apply and evaluate original literature.

The course uses the textbook: Biophysical Chemistry by Klostermeier and Rudolph (CRC Press 2017). We will focus on the “Methods” section (Part IV) of the book, but make frequent references to other areas on the structure and function of proteins. The course includes a fundamental and practical introduction to spectroscopy, thermodynamics, kinetics, scattering and computational analyses that underlies the methods. The course covers a wide range of areas in protein science, including protein structure and folding, protein-protein and protein-ligand interactions and proteome analysis.

27022/26050/26211, Basic knowledge in biochemistry and protein chemistry.

Lectures, e-lectures, exercises, data analysis and computer experiments.

Minimum: 16.

Please be aware that this course will only be held if the required minimum number of participants is met. You will be informed 8 days before the start of the course, whether the course will be held.