Admission requirements
Elective course MSc Chemistry, MSc Life Science and Technology.
Students with a BSc MST/LST or equivalent. Students with a BSc in other subjects should have knowledge of amino acids and protein structure.
This course cannot be combined in a final examination with either Design and Self-assembly of Biomolecules (4423DSBIO) or Protein Folding, Misfolding and Design (4423PFMA).
Description
This course is intended to give students an insight into the fundamentals of protein folding: how proteins achieve and maintain their functional fold in the cellular environment and how disruptions to this process can lead to disease.
A brief recap of protein structure will be given, before the so-called ‘protein folding problem’ will be explained. We will explore how amino acid sequence can direct the assembly of discreet protein structures and how researchers may harness these insights to design new proteins with novel functions.
Then, key differences between folding in the test tube and the cellular environment will be highlighted. Cellular strategies to assist protein folding and combat protein misfolding will be explored through case studies of the molecular chaperones.
The course will wrap up by addressing the risks associated with protein misfolding. We will study examples of human diseases linked to protein misfolding and aggregation (Creutzfeldt-Jakob disease, Alzheimer’s disease, cystic fibrosis,…) and debate the merits of different scientific hypotheses. With the help of recent literature, student will research and present therapeutic strategies currently in development to slow or reverse pathological protein misfolding.
Course Objectives
At the end of this course students will be able to:
Derive from case-studies from the literature, how peptides and proteins can be programmed to form discreet protein structures, and what kinds of functions such structures can fulfil.
Weigh the advantages and disadvantages of de novo design, protein redesign, and computational design in creating new protein structures with novel functions.
Contrast in vitro protein folding and folding in the cell.
Compare the mechanism of action of different families of molecular chaperones.
Explain how protein misfolding can lead to disease and identify appropriate therapeutic strategies to intervene in this process.
Select appropriate analytical techniques to characterize peptide/protein structures and investigate pathological protein aggregation.
Critically evaluate a research papers and present this to the group.
Timetable
Schedule information can be found on the website of the programmes.
You will find the timetables for all courses and degree programmes of Leiden University in the tool MyTimetable (login). Any teaching activities that you have sucessfully registered for in MyStudyMap will automatically be displayed in MyTimeTable. Any timetables that you add manually, will be saved and automatically displayed the next time you sign in.
MyTimetable allows you to integrate your timetable with your calendar apps such as Outlook, Google Calendar, Apple Calendar and other calendar apps on your smartphone. Any timetable changes will be automatically synced with your calendar. If you wish, you can also receive an email notification of the change. You can turn notifications on in ‘Settings’ (after login).
For more information, watch the video or go the the 'help-page' in MyTimetable.
Mode of instruction
Lectures and literature discussion sessions. Students will give presentations in small groups on recent therapies developed to combat protein aggregation diseases.
Assessment method
Written exam (70%), a group presentation on a relevant literature paper (25%), and a computer-based assignment (5%).
Reading list
All relevant literature will be provided on Brightspace at least seven days before the relevant lecture. Students will benefit from reading, in advance, the papers that will be discussed during the lectures.
Registration
Every student has to register for courses with the enrollment tool MyStudyMap. There are two registration periods per year: registration for the fall semester opens in July and registration for the spring semester opens in December. Please see this page for more information.
Please note that it is compulsory to register your participation for every exam and retake. Not being registered for a course means that you are not allowed to participate in the final exam of the course.
Extensive FAQ's on MyStudymap can be found here.
Contact
Remarks
Assignment deadlines are communicated via Brightspace.
According to OER article 4.8, students are entitled to view their marked examination for a period of 30 days following the publication of the results of a written examination. Students should contact the lecturer to make an appointment for such an inspection session.