KJM9250 – Organic NMR Spectroscopy

Lectures include the following topics: Chemical shifts, coupling constants, integraler, relaxation (T1 and T2). Practical aspects for optimization of NMR experiments. Tuning and Matching. Shimming. Selection of acquisition and processing parameters. Information transfer via coupling constants and through space (Overhauser effect). One dimensional and two dimensional pulse sequences. The time dimensions t1 and t2. The frequency dimensions F1 and F2. "Window functions". Intepretation of spectra. Rational choice of type of experiment, acquisition- and processing-parameters in relation to chemical problem. Vector and spin population models in explanation of NMR phenomena and the individual experiment. Inverse detected experiments. The laboratory course (one day each week for 10 weeks) includes the following NMR experiments which are performed by one or two three students together. Pulse angle optimization, selective 1H - 1H decoupling, selective 1D COSY, TOCSY, NOESY and ROESYexperiments, T1/T2 relaxation time determination, DEPT, COSY, TOCSY, HSQC, HMBC, H2BC, HSQC-TOCSY, HSQC-NOESY, NOESY, ROESY and DIFFUSION NMR. One goal is to enhance your competence of setting up new experiments without having a detailed instruction manual in front of you.

After completion of the course:

• You will be able to make a rational choice of type of nmr-experiments for the nuclei; 1H, 13C,19F, 31P and 15N and combinations thereof and can choose and implement acquisition- and processing-parameters in relation to chemical problems.
• You will master vector and spin population models in explanation of nmr phenomena.
• You understand the concepts of tuning/matching and master the practical art of shimming.
• You will understand the concepts of T1- and T2-relaxation and you know how to measure them and how to set up and perform experiments to measure them.
• You understand the concepts of information transfer through electrons in bonds as well as through space via the Overhauser effect. You will understand and can explain the mechanism of the Overhauser effect.
• You understand the concepts of one- and two- dimensional pulse sequences as well as the time dimensions t1 and t2 and the frequency dimensions f1 and f2.
• You understand the concepts of and can apply "window functions" and " linear prediction" in one and two dimensions. You can use non uniform sampling (NUS).
• You understand the differences between inversely and directly detected experiments and know when to choose either of them.
• You will master: pulse angle optimization, selective 1H-1H decoupling, selective COSY, selective TOCSY, selective NOESY, selective ROESY, DEPT(45, 90, 135), COSY(GP), TOCSY(GP),HSQC(EDETGP), HSQC-NOESY, HSQC-TOCSY, HMBCGP, NOESY, ROESY and DIFFUSION NMR experiments.
• You are able to intrepretate and put together information from a series of nmr experiments in elucidation of chemical structures and problems.
• You can explain the effects of magnetic field gradients in nmr-experiments, and how magnetic field gradients make mri-experiments work.

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.

• KJM5280 – NMR Spectroscopy

KJM3000 – Applied Spectroscopy, as well as practical knowledge in acquisition of one dimensional 1H- and 13C-NMR spectra with Bruker Avance instruments using the NMR program TopSpin 1.3.

The course includes 20 hours of lectures and a laboratory course of 50 hours.

The laboratory course must be approved prior to the final examination.

A completed and approved laboratory course is valid for six semesters after the semester it was approved.

It is mandatory to attend the first lecture (including students on the waiting list). If you are unable to attend the first lecture, you must notify the Department of Chemistry before the start of the lecture/exercise, otherwise your course registration will be cancelled and you will lose your place in the course.

Attendance at the laboratory course is mandatory. If you are prevented from meeting, you have to show documentation that you were legally absent (medical note from a doctor or similar).

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.

Access to teaching:

A student who has completed compulsory instruction and coursework and has had these approved, is not entitled to repeat that instruction and coursework. A student who has been admitted to a course, but who has not completed compulsory instruction and coursework or had these approved, is entitled to repeat that instruction and coursework, depending on available capacity.

• Final oral examination (1 hour) which counts 100%

The exam includes tests of practical skills in the laboratory as well as oral examination of theoretical knowledge.

Approved laboratory course is a prerequisite for taking the 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: KJM5250 – Organic NMR Spectroscopy (discontinued)

No examination support material is allowed.

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

This course offers both postponed and resit of examination. Read more:

• Illness at exams / postponed exams
• Withdrawal during an examination / Resitting an examination