MBV9520 – Advanced biomolecular NMR
Course description
Course content
The course will give a practical introduction to NMR spectroscopy and how it is used to obtain structures of small and large proteins.
Structure information is essential for understanding the function of a protein. For proteins 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 resolution obtainable from unlabeled NMR samples is not good enough for proteins for the information to be obtained. To obtain NMR structures of proteins it is practice to label the sample with 15N and 13C, as a result there is a whole array of NMR experiments that can be used to obtain structure information. These experiments use direct J-couplings trough bond to connect spins on neighboring nuclei. Experiments on labeled samples can be used to determine the structure of large proteins.
Learning outcome
Students will learn how to obtain NMR data of labeled proteins on BRUKER NMR instruments. The theory and simple setup of the NMR pulse sequences will be thought. The student should be able to analyze pulse sequences and fix NMR experiments that do not give the wanted outcome. The student will learn to analyze and assign labeled proteins using CARA and automated procedures. Furthermore, the students will learn how to calculate NMR structures using CYANA.
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
The students must have followed the MBV9510 course or have NMR knowledge at similar level.
Overlapping courses
- 10 credits overlap with BIOS9520 – Advanced biomolecular NMR (discontinued).
- 3 credits overlap with BIOS9530 – Biomolecular NMR.
Teaching
The course comprises for each student of 20 lecture hours and 33 hours of lab-exercises. The course is taught intensively for one 9 consecutive days every second year.? A selected set of home work is described that the student should finish and bring to the final exam. Estimated time for this is 1 week of work. 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 before the exam.
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.