After finishing the course the student is able to:
- Describe the main groups of proteins and explain their structure in the context of primary, secondary and tertiary structure, the student has insight into how these come about, and how these differ between the main groups.
- Show insight into the conservation of protein structure in evolution
- Can explain how (fast) proteins fold and describe the role of chaperones in folding
- Understand protein interactions in the context of thermodynamics (and can calculate the relevant thermodynamic parameters) and molecular structure.
- Knows and can recognize the role of specificity and affinity in interactions.
- Explain how ultrasensitive responses come about via cooperativity and allostery and can analyze data in this context.
- Can explain on a basic level how to build organic/polymeric structures for application in nanomedicine.
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The course on biochemistry consists of two parts.
- In the first part by dr. ir. M.M.A.E. Claessens we will discuss how proteins enable the processes of life. We will explore the fundamental principles that allow proteins to function including protein structure and function. We will also discuss how protein structures have evolved (and are still evolving). The function of proteins comes through their interaction with proteins and other molecules. We will investigate how specific targets are recognized and how interactions can result in ultrasensitive responses. Together the topics covered will give you first insights into how proteins control biological processes.
- The second part is taught by dr. ir. J.M.J. Paulusse and deals with the question: How to build organic/polymeric structures for application in nanomedicine? Topics that will be covered are: Polymer chemistry; Characterization of polymers; Well-defined nanostructures; Robust reactions: click chemistry; Controlled polymerization techniques; Nanomedicine.
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