nl en

Fundamentals of NMR Spectroscopy (FNMR)


Fundamentals of NMR Spectroscopy
Up to date schedule information

Elective course in the MSc Chemistry

Admission requirements

Basic knowledge of spectroscopy.


How to prove that an impurity in a batch of medicine is not higher than 0.5%? How to find out the drug binding surface of a protein? What is it that makes nuclear magnetic resonance (NMR) such a powerful analytical technique, able to efficiently answer these and many other questions in chemistry and life sciences?
In this course you will learn the fundamentals of NMR spectroscopy so that you can understand commonly used experiments in chemical or life science research. Emphasis will be on a conceptual understanding of NMR theory, including a classical vector model description, an intuitive quantum mechanical description, origins of relaxation, and multidimensional NMR. In addition, there will be time to gain hands-on experience at a spectrometer.
This course is an obligatory preparation for the NMR courses of the Netherlands Magnetic Resonance Research School.

Course objectives

After the course, the student should be able to:

  • relate the NMR spectrum to an energy diagram and perform elementary calculations;

  • describe and identify the different elements of an NMR experiment;

  • describe and analyze simple NMR experiments using the vector model;

  • describe relaxation in molecular terms;

  • explain how relaxation times can be measured and calculate these;

  • explain and predict the effects of exchange on spectra;

  • use the product operator formalism to analyze NMR experiments;

  • describe how multidimensional NMR experiments are constructed;

  • relate the magnetization transfer mechanisms to the information content of a 2D experiment.

  • interpret a 2D spectrum.


Course 1: Spins in the magnetic field (HvI/GS)
Course 2: Vector model description of NMR (GS)
Course 3: FT-NMR (GS)
Course 4: The 1D NMR spectrum (GS)
Course 5: Relaxation (HvI)
Course 6: NOE (HvI)
Course 7: Product operator formalism (HvI)
Course 8: Magnetization transfer mechanisms (HvI)
Course 9: Multidimensional NMR (HvI)
Course 10: Basic 2D experiments (GS)
Course 11: Demo @ NMR machine (GS)
Course 12: Chemical and conformational exchange (HvI)
Course 13: Protein interaction studies (HvI)

Mode of instruction

Weekly lectures and exercise sessions, a practical at the NMR machine during one of the exercise sessions, a computer NMR simulation practical (in lecture 13) and a demonstration at the NMR machine of advanced theoretical concepts (in lecture 11).

Assessment method

Written exam (3hrs).
The exam includes a hand-out with values of physical constants, and a selection of formulas.


All students should and register to the course on Blackboard.
Blackboard is used as a standard way of communicating with the students, both for the slides, a syllabus, the exercises, and the answers to the exercises. An exam example will be published on Blackboard as well, together with the answers, for self-study.

Reading list

  • “Understanding NMR Spectroscopy” (2nd Edition, 2010) by James Keeler, John Wiley and Sons, England; ISBN: 978-0-470-74609-7

  • hand-out of slides and a syllabus will be provided at the course via Blackboard.


Exchange and Study Abroad students, please see the “Prospective students website”: for information on how to apply.
All students should and register to the course on Blackboard.

Registration for the exam via uSis is compulsory (als je een schriftelijk tentamen geeft)

Contact information

Dr. Hugo van Ingen
Protein Chemistry
Room HB 0.26
Tel. 071-5271037


In theory, there is no difference between theory and practice. In practice, this is only true for NMR.