BIOS9520 – Advanced biomolecular NMR

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.

The students must have followed BIOS9510 – Biomolecular NMR Spectroscopy (discontinued) or have NMR knowledge at similar level.

Overlapping courses

Teaching

  • 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

As?the?teaching involves laboratory and/or field work, you should consider taking out a separate travel and personal risk insurance.?Read about your insurance cover as a student.

Examination

  • ?Final oral examination counting 100% after course ending.

  • Participation and laboratory journals must? be approved before the exam.

Withdrawal from an examination?

It is possible to take the exam up to 3 times. It will?be counted as one of the three attempts to sit the exam for this course, if you sit the exam for one of the following courses: MBV9520 – Advanced biomolecular NMR (continued) and BIOS9530 – Biomolecular NMR.

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

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

Last updated from FS (Common Student System) Dec. 22, 2024 4:23:18 AM

Facts about this course

Level
PhD
Credits
5
Teaching
Spring

Every other spring

The course is last held spring 2021

Examination
Spring

Examination is last held spring 2021

Teaching language
English