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.
In MyTimetable, you can find all course and programme schedules, allowing you to create your personal timetable. Activities for which you have enrolled via MyStudyMap will automatically appear in your timetable.
Additionally, you can easily link MyTimetable to a calendar app on your phone, and schedule changes will be automatically updated in your calendar. You can also choose to receive email notifications about schedule changes. You can enable notifications in Settings after logging in.
Questions? Watch the video, read the instructions, or contact the ISSC helpdesk.
Note: Joint Degree students from Leiden/Delft need to combine information from both the Leiden and Delft MyTimetables to see a complete schedule. This video explains how to do it.
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
As a student, you are responsible for enrolling on time through MyStudyMap.
In this short video, you can see step-by-step how to enrol for courses in MyStudyMap.
Extensive information about the operation of MyStudyMap can be found here.
There are two enrolment periods per year:
Enrolment for the fall opens in July
Enrolment for the spring opens in December
See this page for more information about deadlines and enrolling for courses and exams.
Note:
It is mandatory to enrol for all activities of a course that you are going to follow.
Your enrolment is only complete when you submit your course planning in the ‘Ready for enrolment’ tab by clicking ‘Send’.
Not being enrolled for an exam/resit means that you are not allowed to participate in the exam/resit.
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.
Software
Starting from the 2024/2025 academic year, the Faculty of Science will use the software distribution platform Academic Software. Through this platform, you can access the software needed for specific courses in your studies. For some software, your laptop must meet certain system requirements, which will be specified with the software. It is important to install the software before the start of the course. More information about the laptop requirements can be found on the student website.