MBV9510 – Biomolecular NMR Spectroscopy

Schedule, syllabus and examination date

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Course content

The course will give a practical introduction to NMR spectroscopy and how it is used to obtain structures of peptides and small proteins.

Structure information is essential for understanding the function of a protein. For small proteins and peptides that are difficult or impossible to crystallize NMR spectroscopy is the method available for 3D structure determination.

In NMR spectroscopy resonance frequency, intensity and correlation is measured. These spectroscopic qualities contain structural information. It is this structural information that is used in structure calculations that in the end give the NMR structures. The information is available in the NMR spectra, however, to be use full one need to obtain NMR spectra and determine where NMR signals come from. The later is in NMR spectroscopy called the assignment process. The course will have lectures in biomolecular NMR acquisition and assignment of 1D and 2D NMR spectra of water containing samples.

Learning outcome

Students will learn how to obtain NMR data of unlabeled proteins and peptides dissolved in water on BRUKER NMR instruments. The student will learn to analyze and assign 2D COSY, TOCSY and NOESY spectra using modern computer tools. Furthermore, the students will learn from what sort of data NMR structures are calculated and how. The students will be thought how to evaluate the quality of NMR structures.


PhD candidates from the University of Oslo should apply for classes and register for examinations through Studentweb.

If a course has limited intake capacity, priority will be given to PhD candidates who follow an individual education plan where this particular course is included. Some national researchers’ schools may have specific rules for ranking applicants for courses with limited intake capacity.

PhD candidates who have been admitted to another higher education institution must apply for a position as a visiting student within a given deadline.


Recommended previous knowledge

Basic knowledge of protein structure.

Overlapping courses

No overlap with other courses


The course comprises for each student of 22 lecture hours and 38 hours of lab-exercises. The course is thought intensively for 9 consecutive days every second year. First time taught February 2011.
Selected articles should be studied before course start. Selected exercises should be finished after the course and brought to the final exam. Estimated time for this activity: one week and a half.
All teaching sessions are obligatory and constitute the curriculum together with hand-outs and pre-defined articles.


Approved participation and laboratory journals. Final oral examination counting 100% after course ending.

Examination support material

No examination support material is allowed.

Grading scale

Grades are awarded on a pass/fail scale. Read more about the grading system.

Explanations and appeals

Special examination arrangements

Application form, deadline and requirements for special examination arrangements.


The course was earlier part of the BioStruct PhD-school (National Graduate School in Structural Biology) with the course code MBV9510BIOSTRUCT

Facts about this course






Every second spring semester


Every second spring semester

Teaching language


Please contact Per Eugen Kristiansen for information about the course