Universität Wien

323115 VU NMR for Drug Design - MPS5 (2024W)

2.00 ECTS (1.00 SWS), SPL 32 - Pharmazie
Continuous assessment of course work

Anmeldung bis 08.12.2024 möglich !

13.01.2024 9:00-12:00 2D313
14.01.2024 9:00-12:00 2D313
16.01.2024 9:00-12:00 2D313
17.01.2024 9:00-12:00 2D313
Moodle

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Note: The time of your registration within the registration period has no effect on the allocation of places (no first come, first served).

Details

Language: English

Lecturers

Classes

13.01.2024 9:00-12:00 2D313
14.01.2024 9:00-12:00 2D313
16.01.2024 9:00-12:00 2D313
17.01.2024 9:00-12:00 2D313

Information

Aims, contents and method of the course

Protein-ligand interactions are at the heart of drug discovery research. NMR spectroscopy is perfectly suited to identify and validate protein-ligand interactions. A large number of NMR experiments are available. They are very powerful, but may also have pitfalls and limitations.
In this lecture, we will present central experiments for NMR in drug discovery, and assess their strengths and reliabilities.
Furthermore, methods for subsequent characterization of the interaction such as quantitative KD determination, binding mode analysis, or structure determination will be covered if time allows.

Assessment and permitted materials

The primary performance required is a scientific presentation (PowerPoint) based on assigned primary literature, followed by a defense/Q&A session. You must demonstrate the ability to deconstruct a peer-reviewed paper, explaining the choice of NMR methods used by the authors and the validity of their conclusions. Regarding aids, you are permitted to use the original research paper, your prepared slides, and any supplementary data provided in the literature during your presentation.

Minimum requirements and assessment criteria

To achieve a positive assessment, you must deliver a coherent presentation that covers the study’s objectives, NMR methodology, and results. A "Pass" requires demonstrating (1) Basic knowledge of NMR and the ability to handle technical questions during the discussion. It is strongly recommended that students have completed 322052-1 Basics of NMR Spectroscopy (M14), as the fundamental physics of spins will not be re-taught. Grading is based on the clarity of the presentation, the accuracy of your methodological critique, and the depth of your answers during the Q&A. A grade of "1" (Excellent) is reserved for those who can identify subtle pitfalls in the paper's data, while a "4" (Sufficient) is given if the basic experimental setup is understood but the defense is weak.

Examination topics

The exam evaluates four key pillars of expertise through the lens of your assigned paper:
Theoretical Mastery: You must explain the physics of the specific experiments used in the paper, such as ligand-observed (STD, WaterLOGSY, CPMG) or receptor-observed (HSQC-CSP) techniques.
Practical Application: You must be able to explain how the authors derived the Dissociation Constant and how they mapped binding pockets using Chemical Shift Perturbations (CSPs).
Critical Evaluation: You are expected to critique the study's limitations, for example, explaining why certain fragments might have yielded false positives in an STD experiment or if the was outside the optimal NMR sensitivity range.
Scientific Communication: You must translate complex NMR spectra into clear, biological conclusions regarding the drug’s binding mode and affinity.

Reading list

To achieve the learning objectives, the following core literature is recommended:

Primary Textbook: NMR in Drug Design (various authors, e.g., David J. Craik or Oliver Zerbe).

Reference Book: Protein-Ligand Interactions: Methods and Applications (Methods in Molecular Biology series).

Key Review Article: "Perspectives on NMR in drug discovery: a technique comes of age" (Pellecchia et al., Nature Reviews Drug Discovery).

Supplemental Material: Provided lecture slides and selected scientific papers (e.g., original papers on STD-NMR by Mayer & Meyer).

Association in the course directory

Last modified: Th 19.02.2026 00:29