Schedule, syllabus and examination date

Course content

The course will give a introduction to interpretation of NMR data for structure determination 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. It, furthermore, is a method that makes information with regards to protein ligand structures easy to obtain.

To use this information the spectra obtained needs to be assigned. Different NMR samples and sizes of proteins require different strategies for assignment.

Learning outcome

After finishing the course you will:

  • Know what samples one need for NMR analysis of peptides, proteins and their interactions.

  • Be able to calculate and evaluate NMR structures from spectral data using methods programs such as CYANA, water refinement and PDBstat.

  • Have knowledge with regards to the selection of methods for protein ligand interaction studies.

  • Be able to determination of structures of protein ligand interactions, using HADDOCK

  • Master assign a small peptide using techniques 2D COSY, TOCSY, NOESY, 15N HSQC and 13C HSQC.

  • Master assign a 15N labeled protein.

  • Master assign a 13C and 15N labeled protein using spectra such as HNCO, HNCA, HNcoCA, HNcaCO, HNCACB, HNcoCACB, HCCH-TOCSY etc.

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.

Please contact Dr.Scient Per Eugen Kristiansen for more information about the course or Jon-Arne Bilben Haugseth?for questions about admission.

Only students admitted to the course may take part in instruction and tuition and sit for the examination.

The students should have followed the BIOS4020 course or have NMR knowledge at similar level.

Overlapping courses

Teaching

  • 16 lecture hours

  • 44 hours of computer lab-exercises.

A selected set of homework is described that the student should finish and bring to the final exam.

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.

This course has mandatory exercises that must be approved before you can sit the final?exam.

It will also 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:?MBV9510 – Biomolecular NMR Spectroscopy (continued), MBV9520 – Advanced biomolecular NMR (continued), BIOS9510 – Biomolecular NMR Spectroscopy (discontinued) and BIOS9520 – Advanced biomolecular NMR (discontinued).

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.

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 9:59:00 AM

Facts about this course

Level
PhD
Credits
5
Teaching
Spring
Teaching language
English

Contact

Department of Biosciences