Key information

Next planned course: April 12-16, 2021
Registration deadline: February 15, 2021 (now closed)
Location: Digital course, hosted by NTNU
Course responsible: Professor Finn L. Aachmann

Grading: Evaluation of lab reports (pass/fail)
Credits: 5 ECTS

Registration is now closed. The instructions below are for reference purposes only.

Both of the steps below should be completed if you want to register and receive credits for this course:

  • Register to BioCat using the form at the bottom of this page
  • Contact Professor Finn Aachmann and inform him of your registration.

Admission

In order to attend this course, participants should document basic understanding of protein NMR, i.e. fulfill the learing outcome of C11 Protein NMR I, structure determination.

Tentatively for 6-8 students, with a maximum number of 10 participants.

Content

This course will provide students with sufficient basic knowledge in protein NMR to pursue dynamic applications; including relaxation measurements, kinetic tracking of enzyme-mediated substrate conversion.

The two NMR courses within BioCat have a modular organization, where the first module at UiB (C11 Protein NMR I, Structure determination) primarily concerns protein-NMR basics up to structural characterization, while the next module (C12 Protein NMR II, Functional characterization; this course) at NTNU, focuses on functional enzyme characterization, including enzyme kinetics and dynamics.

Teaching

The course will be taught intensively over five days. The students will acquire basic knowledge of functional characterization by NMR through a combination of theoretical background, lectures, practical exercises, as well as case studies from relevant literature.

Thus, the overall aim of the course is for the participants to gain hands-on experience while performing experiments. They will also learn how to set up real experiments that could then be implimented at their home institutions or other facilities.

On-site tentative schedule (digital schedule may vary slightly)

Day 1: 

Short icebreaker section followed by basic introduction and motivation for studing the function of proteins. Hereafter, a lecture on structural elucidation of carbohydrates. This should provide the students with basic knowledge on structural elucidation of different carbohydrates. In the afternoon, the students will have practical exercises where they will assign different carbohydrates. (Course material: Review articles and compendium)

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 moring section. The students will be divided into two groups and carry pratical exercises on theNMR instrument in the afternoon. (Course material: Articles, book {High-Resolution NMR Techniques in Organic Chemistry, 3rd Edition, Timothy D.W. Claridge} and compendium)

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 analyse the data form such experiments. (Course material: Articles and compendium).

MondayTuesdayWednesdayThursdayFriday
09.00 – 12.00Introduction and motivation Carbohydrate assignment (Finn L. Aachmann)Ligand NMR and chemical exchang (Rienhard Wimmer, Aalborg university)Ligand NMR and pH (Finn L. Aachmann and Gaston Courtade)Protein dynamics (Johan Isaksson, UiT)Time-reesolved NMR (Finn L. Aachmann and Gaston Courtade)
13.00 – 16.00Practical exercisesSet up STD, T1p, WaterlogsySetup Ligand and pH titrationsSet up T1, T2 and NH-NOE CEST, REXSet up enzymatic reeaction and extract kinetic parameeteers

The students are expected to spend 2-3 hours after class each afternoon to summarize the day and prepare for the following day.

Work requirement

According to generic ECTS guidelines, students should be prepared to dedicate 25-30 working hours pr. study point. In this course the workload is distributed into:

  • 25 hours: Preparation for lectures and lab exercises (before course and on site)
  • 15 hours: Lectures (on site)
  • 15 hours: Laboratory exercises (on site)
  • 80 hours: Finishing reports and exam preparations

Exam and evaluation

Evaluation of lab report generated from results obtained during the pratical part of the course. All lab reports should be approved within 2 months in order to pass the course. 

Syllabus

Course material will be provided during the course

Learning outcome

This course aims to enable the candidate to propose a reasonable strategy for functional characterization of proteins by NMR spectroscopy. The candidates will gain hands-on experience through performing experiments as well as they will also learn the theoretical background from the lectures.

Knowledge

By the end of this course, the students will have:

  • Knowledge of strategies for functional characterization of proteins by NMR spectroscopy and an understand of their strengths/limitations
  • Basic knowledge on assignment strategies for small organic compounds (protein ligands).
  • Familiarity with theoretical background and experimental setup for ligand interaction, pH, Chemical exchange and protein dynamics.
  • Familiarity with the toolbox of programs for functional characterization of proteins

Skills

By the end of this course, the students will be able to:

  • Evaluate the applicability of functional characterization of proteins by NMR spectroscopy, particularly for functional characterization of proteins
  • Select the relevant experimental setup for functional characterization of proteins
  • Evaluate the experimental data with programs and make graphical display
  • Propose and design an experiment workflow for functional characterization of proteins

General competence

During this course, the student will gain experience in:

  • Critical evaluation of literature of functional characterization of proteins by NMR spectroscopy and extraction of information from primary literature sources
  • Scientific writing skills
  • Experimental planning

Registration is now closed.