Course Syllabus

Welcome to course KEM840 NMR Spectroscopy for Students of Pharmacy!

 

The course starts March 21, 09.00 in the lecture room on ground floor at the Swedish NMR Centre, Medicinaregatan 5c. It is important that you can attend the course start, it is at this time you get essential information regarding how the course will be organized. This occasion cannot be retaken.

It is important that you register on the course in Ladok. The self-registration can be done on Ladok in the Student Portal one week prior to course start until the 18th of March.

 

Information about the course

Schedule

Course literature and syllabus you find on the website here.

 

 

NMR Spectroscopy for Students of Pharmacy

7.5 hp COURSE, VT 2024, Dept. of Chemistry and Molecular Biology

Course language: English

Head of the course
Göran Karlsson (GK); goran.karlsson@nmr.gu.se
Swedish NMR Centre & Dept. of Chemistry and Molecular Biology

Teachers
Göran Karlsson (GK) goran.karlsson@nmr.gu.se
Vladislav Orekhov (VO) vladislav.orekhov@gu.se
Arthur Pinon (ACP) arthur.pinon@gu.se
Anders Bay Nord (ABN) anders.bay.nord@nmr.gu.se
Cecilia Persson (CP) cecilia.persson@nmr.gu.se
Ulrika Brath (UB) ulrika.brath@nmr.gu.se
Ashish Kawale (AK) ashish.kawale@nmr.gu.se
Weixiao Wahlgren (WW) weixiao.yuan.wahlgren@gu.se

Location
Lectures, seminars, laborative excercises and diagnostic tests take place at the Swedish NMR Centre, Medicinaregatan 5c, Göteborg

Aim
NMR (nuclear magnetic resonance) is a widely used analytical method. Application areas range from material science to advanced analysis of biological macromolecules, metabolomics and imaging techniques. NMR techniques are routinely applied in organic chemistry, natural product chemistry and drug development.
The aim of the course is to provide enhanced knowledge about NMR spectroscopic techniques that are used for drug development and the identification of drug-like substances, for assessment of purity and for the analyses of their interaction with proteins. The course will also provide an insight into NMR theory and more general applications of NMR methodology.

Literature
High-Resolution NMR Techniques in Organic Chemistry, 3rd edition, T. W.D. Claridge, Elsevier.
Articles/chapters/ tasks/handouts distributed during the course by the lecturers.
Information on CANVAS:
- schedule, tasks, specific info
- slides/handouts from lectures
- practicals
- problems for solving
- hand-in practical reports and other assignments

Examination 
- Seminars (participate, present and discuss explanatory task, pass or fail; a written report is required on fail)
- The summary result on four  diagnostics tests (dugga) (pass ≥50% or fail <50%)
- Written report on laborative exercises (practicals) – (pass or fail)

Final mark for the course
The final mark will be based on sum of the four diagnostic tests (VG ≥ 75%, 50% < G < 75%, U< 50%)

COURSE OVERVIEW
Lectures  will address 1D and 2D NMR for small molecules and include the concepts of J-coupling, chemical exchange, relaxation, the nuclear Overhauser effect. 1D and 2D NMR techniques (e.g. COSY, NOESY, HSQC, HMQC) will be explained and presented on the framework of the vector, as well as the concept of fragment based screen and reverse screening. NMR in structural biology, metabolomics, pharmaceutical applications as well as new development is presented.  

Laborative exercises (practicals)  will give hands on experience in sample handling, setting up and running 1D and 2D homonuclear and heteronuclear NMR experiments, processing and analysis of 1D and 2D NMR spectra for the structure identification of small molecules as well as for ligand protein interaction studies.

Explanatory tasks will be handed out during the course. The tasks will be presented by the students (groups of two students) at the seminars.

Seminars will give additional insight in problem solving, analysis of NMR spectra and modern NMR research literature.

Lectures, (chapter in text book) teacher
Introduction to NMR, (2.1-2.5.2) GK
 Practical Aspects of HRN, (3.1-3.6) VO
One-dimensional techniques, (4.1.1-4.1.2, 4.2-4.4.2) GK
Two-dimensional  NMR, (5.1-5.2) GK
2D COSY & TOCSY, (6.1-6.2) VO
HSQC, HMQC& HMBC, (7.1-7.4) GK
Exchange and dynamics, (2.6) GK
NOESY, (9.1-9.6) VO
Structure elucidations and spectrum assignment, (13.1-13.9) GK
Pure-shift, quantitative aspects, DNP, PRE, diffusion NMR, (8.6, 10.1-10.2) VO
Applications of solid-state NMR in pharmaceutical development ACP
Fragment Based Screen Applications GK
Metabolomics ABN
Protein NMR GK
            

Seminars:    
J-coupling
Questions and presentation of problems 1
Questions and presentation of problems 2
Questions and presentation of problems 3
Questions and presentation of problems 4

Computer laborative exercises  (Practicals):
Processing of 1D data
Setting up and running 1D NMR
Processing of 2D data
Setting up and running 2D NMR
Analysis and molecular assignment
Fragment based screen
Solid State NMR and DNP-NMR

A written report has to be handed in within eight (8) days of the laborative exercise 1-5. 
Check the schedule for precise information.

 

 

Contact

Course leader: Göran Karlsson.

Course administrator: Alexander Englund

Study councelor: Per Martin Björemark

The study expedition is at Natrium, room 2101 and has the following opening hours:

•  Tuesdays and Thursdays 12:30-15:00

Students with a NAIS statement should contact the study councelor in the beginning of the course in order to receive the support that is recommended in the statement.

For more information about the department and about the university rules continue to Student Portal: https://studentportal.gu.se/en/organization/department-of-chemistry-and-molecular-biology