Protein science: Structure, interactions and molecular properties
Overall Course Objectives
The course provides a broad introduction to molecular protein science with focus on methods used to characterize the structure, stability and interactions of proteins. We will work with the theoretical underpinnings of the measuring principles, application of the methods and critical assessment of the results. This will include a thorough discussion and evaluation of the forces and mechanisms that stabilize protein conformations and protein-ligand complexes. The course will present a modern view into how method selection is performed in protein science. The student will also learn how analysis of collected data drives the decision-making process forward, towards the next step in a research project.
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Learning Objectives
- 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.
Course Content
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.
Teaching Method
Lectures, e-lectures, exercises, data analysis and computer experiments.
Faculty
Limited number of seats
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.