MBV9510 – Biomolecular NMR Spectroscopy

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.

Admission to the course

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

• 10 credits overlap with BIOS9510 – Biomolecular NMR Spectroscopy (discontinued).
• 3 credits overlap with BIOS9530 – Biomolecular NMR.

Teaching

•  22 lecture hours and 
• 38 hours of lab-exercises. The course is thought intensively for 9 consecutive days every second year.  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.

Examination

• Final oral examination counting 100% after course ending. Participation and laboratory journals must  be approved befor the exam. 

Examination support material

No examination supprt material is alloved.

Grading scale

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

Resit an examination

Students who can document a valid reason for absence from the regular examination are offered a postponed examination at the beginning of the next semester. Re-scheduled examinations are not offered to students who withdraw during the original examination.

More about examinations at UiO

• Use of sources and citations
• Special exam arrangements due to individual needs
• Withdrawal from an exam
• Illness at exams / postponed exams
• Explanation of grades and appeals
• Resitting an exam
• Cheating/attempted cheating

You will find further guides and resources at the web page on examinations at UiO.