Admission requirements
Core course in MSc Chemistry - Chemical Biology, core course in MSc Life Science and Technology (Biophysical Sciences series), elective course.
For students with a BSc MST, LST or equivalent. Good understanding of protein structure (primary – quaternary structure, amino acids), basics of Michaelis Menten kinetics, concept of Boltzmann equilibrium is needed.
Description
Proteins carry out most functions in the cell. These molecules are not rigid, but are mobile on a wide range of timescales. The course aims to convey the concept of protein dynamics in relation to biological function. The focus is on enzyme catalysis and two techniques will be discussed in detail: nuclear magnetic resonance (NMR) spectroscopy to study protein mobility and kinetic measurements to characterise enzyme activity. NMR spectroscopy is a versatile analytical technique with many applications. We will discuss the fundamentals of NMR (chemical shift, dipolar coupling, J-coupling, relaxation), as well as multidimensional NMR and relaxation experiments to characterize molecular mobility on nanosecond and millisecond timescale. It provides a basis in NMR spectroscopy that is of use for any chemist. The study of kinetics will comprise steady state and pre-steady state theory and methods to measure enzyme characteristics such as k(cat) and K(M), as well as inhibitor kinetics. The theory will be placed into context by studying several papers from the literature.
Course objectives
Learning goals:
the student understands the fundamentals of NMR spectroscopy and can explain the concepts of chemical shift, dipolar coupling, J-coupling, relaxation and chemical exchange
the student understands how NMR spectroscopy can be used to study protein dynamics on different timescales and can critically discuss possibilities and limitations
the student understands and can apply the theory of steady state and pre-steady state kinetics for the characterisation of enzyme-catalysed reactions in calculations and simulations
the student can explain how kinetic experiments are performed and analysed, both for steady state and stopped-flow measurements
the student understands the concept of dynamics in enzymology and can apply this knowledge to explain results described in the literature as well as to address questions concerning new systems
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, exercises, discussions and simulations. We will work with a flipped class-room approach for some aspects of the course.
Assessment method
Exercises and an online test need to be completed and handed in to be allowed to participate in the written exam at the end of the course.
Written exam (closed book) with admission requirement.
Reading list
Required book: Peter Hore, Nuclear Magnetic Resonance, Second Edition, ISBN: 9780198703419, Oxford Chemistry Primers.
Links to the relevant literature articles will be published on Brightspace.
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.