MBV9510 – Biomolecular NMR Spectroscopy

Schedule, syllabus and examination date

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Changes in the course due to coronavirus

Autumn 2020 we plan for teaching and examinations to be conducted as described in the course description and on semester pages. However, changes may occur due to the corona situation. You will receive notifications about any changes at the semester page and/or in Canvas.

Spring 2020: Teaching and examinations was digitilized. See changes and common guidelines for exams at the MN faculty spring 2020.

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.

Basic knowledge of protein structure.

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.

Special examination arrangements, use of sources, explanations and appeals

See more about examinations at UiO

Last updated from FS (Common Student System) Aug. 4, 2020 2:15:27 PM

Facts about this course

Credits
5
Level
PhD
Teaching
Spring

Every other spring

Examination
Spring
Teaching language
English