Course - Functional enzyme characterization using NMR (C12) - BT8136
BT8136 - Functional enzyme characterization using NMR (C12)
Examination arrangement: Portfolio
Grade: Passed / Not Passed
This course will provide students with sufficient knowledge in protein NMR to pursue functional enzyme characterization using NMR This includes ligand interaction analyses, relaxation measurements, protein dynamics and kinetic tracking of enzyme-mediated substrate conversion.
- Select a suitable assignment strategy for structural elucidation of substrate molecules.
- Select relevant methodology to probe functional aspects of proteins by NMR
- Select time-resolved methods for studying enzymatic conversion of molecules.
- Plan, setup and justify functional protein studies by NMR
- Assess other functional studies of proteins and suggest appropriate functional studies by NMR
- Carry out functional characterization studies by NMR
- Process NMR data using relevant software and scripts
- Combine functional information on protein obtained by NMR spectroscopy.
Learning methods and activities
The course includes both theory and practical experiments and it is the aim of the course that the students will gain hands on experience with the different techniques. They will also learn how to set up real experiments that could then be implemented at their home institutions.
Day 1: Short icebreaker section followed by basic introduction and motivation for studying the function of proteins. Hereafter, a lecture on structural elucidation of substrate molecules. This should provide the students with basic knowledge on structural elucidation of different types of substrates. In the afternoon, the students will have practical exercises where they will assign different substrates.
Day 2-4: Each day will deal with one subtopic within functional studies of proteins by NMR, where the theoretical background as well as case studies form literature will be taught in the morning section. The students will be divided into two groups and carry practical exercises on the NMR instrument in the afternoon.
Day 5: Introduction to time-resolved NMR and its application. Theoretical background for pseudo 2D and 3D experiments as well as their potential, limitation, and pitfalls. In the afternoon, the students will set up and follow an enzymatic reaction over time by using the NMR instrument. They will learn how to extract and analyses the data form such experiments.
Further on evaluation
Evaluation of lab report generated from results obtained during the practical part of the course. All lab reports should be approved within 2 months to pass the course.
Admission to a programme of study is required:
Required previous knowledge
The students should document basic understanding of protein NMR equal to BioCat C11 course on protein structure determination by NMR. The course builds on basic understanding of protein NMR. For the functional characterization, the theoretical part of the course will be organized as lectures and followed up by group work with practical exercises using the NMR instruments and at times, also using case studies from relevant literature.
High-Resolution NMR Techniques in Organic Chemistry, 3rd Edition, Timothy D.W. Claridge
Review articles and compendium
Credits: 5.0 SP
Study level: Doctoral degree level
Term no.: 1
Teaching semester: SPRING 2024
Language of instruction: English
- Technological subjects
Examination arrangement: Portfolio
- Term Status code Evaluation Weighting Examination aids Date Time Examination system Room *
- Spring ORD Portfolio 100/100
Room Building Number of candidates
- * The location (room) for a written examination is published 3 days before examination date. If more than one room is listed, you will find your room at Studentweb.
For more information regarding registration for examination and examination procedures, see "Innsida - Exams"