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700MHz AVNEO NMR Spectrometer, Bruker

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Universität Wien

Vienna | Website

Open for Collaboration

Kurzbeschreibung

Nuclear Magnetic Resonance (NMR) has become pivotal for understanding biomolecular structures, particularly in proteins and nucleic acids, offering insights into interactions and functional processes, even within living cells. It integrates structural, dynamic, kinetic, and thermodynamic data, making it indispensable for cutting-edge medical and biological research. Solution NMR plays a vital role in elucidating molecular interactions crucial for cellular functions, aided by recent hardware and software advancements. Its versatility spans from supra-molecular to intrinsically unfolded proteins, facilitating the study of dynamic processes across various timescales. The NMR platform alleviates the workload for researchers and promotes the democratization of bio-NMR studies, thus driving progress in structural biology.

A 700MHz NMR spectrometer equipped with a TCI probe enhances drug design and structural biology by providing high-resolution data on the structure and dynamics of biomolecules like proteins and nucleic acids. This enables researchers to elucidate molecular interactions between potential drug candidates and their targets, aiding in the rational design of novel therapeutics. Additionally, the instrument's sensitivity and versatility allow for the characterization of complex biomolecular structures, providing valuable insights into their function and behavior, crucial for understanding disease mechanisms and developing effective treatments.

Ansprechperson

Julien Orts

Research Services

The service includes setting up NMR experiments, either as routine procedures or through collaboration for more complex tasks. Additionally, students receive training to operate the NMR machines.

Methoden & Expertise zur Forschungsinfrastruktur

One application of a 700MHz NMR spectrometer equipped with a TCI probe is elucidating the structure of a protein-ligand complex in drug design. Researchers can use the high-resolution data obtained from the spectrometer to determine the three-dimensional structure of the protein and the binding mode of the ligand. This information is crucial for understanding the molecular interactions between the protein and the drug candidate, facilitating the rational design of more potent and selective therapeutics.

Nutzungsbedingungen

Access to the NMR facility can be arranged through the Department of Pharmaceutical Chemistry at the University of Vienna, as detailed on their website: https://pharmchem.univie.ac.at/facilities/nmr-spectroscopy/.

Kooperationspartner

(non-exhaustive)
The Research Institute of Molecular Pathology
Astrazeneca
Astex
ETH Zurich
University of Padova
Monash University
University of Queensland
Goethe University Frankfurt
University of Geneva

Referenzprojekte

A calorimeter at atomic resolution
2023 ERC-COG
Julien Orts

“ALLODD – Allostery in Drug Discovery”.
H2020-MSCA-ITN-2020
Christoph Rademacher

“Modulation of platelet biology with CLEC-2 targeted liposomes”,
WWTF Chemical Biology, LS21-039,
Christoph Rademacher

Referenzpublikationen

Altincekic, N., et al., Targeting the Main Protease (M(pro), nsp5) by Growth of Fragment Scaffolds Exploiting Structure-Based Methodologies. ACS Chem Biol, 2024. 19(2): p. 563-574.

Wasilewicz, A., et al., Identification of Natural Products Inhibiting SARS-CoV-2 by Targeting Viral Proteases: A Combined in Silico and in Vitro Approach. J Nat Prod, 2023. 86(2): p. 264-275.

Shanina, E., et al. 2022). Targeting undruggable carbohydrate recognition sites through focused fragment library design. Communications Chemistry, 2022, 5, 64.

Shanina, E., et al., Druggable Allosteric Sites in beta-Propeller Lectins. Angew Chem Int Ed Engl, 2022, 61(1), e202109339.

Kontakt

Julien Orts
Faculty of Life Sciences
https://bionmr.univie.ac.at/

Standort

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