Generic Symposium



2020 Virtual NMR Symposium

Session 1
  (8:00 – 10:50 am)

8:00 AM


Detection of metabolic reprograming associated with HBV infection using metabonomics

Prof. Yulan Wang,

Singapore Phenome Center

    [ abstract ]

8:40 AM


NMR As Mechanistic Tool In Photocatalysis

Prof. Ruth M. Gschwind,

University of Regensburg

    [ abstract ]

[1] C. Feldmeier, H. Bartling, E. Riedle, R.M. Gschwind, J. Magn. Res., 2013, 232, 39.
[2] C. Feldmeier, H. Bartling, K. Magerl, R.M. Gschwind, Angew. Chem. Int. Ed., 2015, 54, 1347.
[3] H. Bartling, A. Eisenhofer, B. König, R.M. Gschwind, JACS 2016, 138, 11860-11871.
[4] A. Seegerer, P. Nitschke, R.M. Gschwind, Angew. Chem. Int. Ed. 2018, 57, 7493-7497.
[5] L. Nanjundappa, A. Seegerer, J. Hioe, R.M. Gschwind, JACS 2018, 140, 1855-1862.
[6]. S. Wang, L. Nanjundappa, J. Hioe, R. M. Gschwind, B. König, Chem. Sci., 2019, 10, 4580.
[7] N. Berg, D. Horinek, R.M. Gschwind, submitted.

9:20 AM


Ultraclean pure shift NMR?

Prof. Gareth Morris,

University of Manchester

    [ abstract ]

No experimental technique is perfect: any NMR experiment, from pulse-acquire up to the most sophisticated solid-state experiments, requires compromises to be made between sensitivity, resolution, ease of use, quantitativity, spectral purity, etc. PSYCHE is successful because it offers a particularly favourable trade-off between the first three of these desiderata and the remaining two. In particular, it allows the user to choose the most appropriate compromise between sensitivity and spectral purity by varying the flip angle ? of the two “chirp” pulses used. The intensity of the pure shift signals is proportional to sin2?, while that of “recoupling” artefacts at ±1/2 Hz either side is proportional to sin4?. For a dilute sample where we are struggling for signal-to-noise ratio we can use a high ?, since the artefacts will be hidden by the noise, but for a high dynamic range sample we would use a low ?, to avoid recoupling artefacts being confused with the signals of dilute species.

To date, the need for this compromise has simply been accepted. But if it were possible to suppress the recoupling artefacts, we could have a PSYCHE experiment with simultaneously improved sensitivity, resolution, and spectral purity . . .

1. “Ultra-high resolution NMR spectroscopy”. Mohammadali Foroozandeh, Ralph W. Adams, Nicola Meharry, Damien Jeannerat, Mathias Nilsson and Gareth A. Morris, Angew. Chem., Int. Ed. 53, 6990-6992 (2014). DOI: 10.1002/anie.201404111.
2. “Ultrahigh-resolution Total Correlation NMR Spectroscopy”. Mohammadali Foroozandeh, Ralph W. Adams, Mathias Nilsson and Gareth A. Morris, J. Am. Chem. Soc. 136, 11867-11869 (2014). DOI: 10.1021/ja507201t.
3. “PSYCHE Pure Shift NMR Spectroscopy”. Mohammadali Foroozandeh, Gareth A. Morris and Mathias Nilsson, Chem. Eur. J. 24, 13988 – 14000 (2018). DOI: 10.1002/chem.201800524.
4. “Pure Shift NMR Spectroscopy”, Ralph W. Adams, eMagRes 3, 1–15 (2014). DOI 10.1002/9780470034590.emrstm1362.
5. “Broadband 1H homodecoupled NMR experiments: Recent developments, methods and applications”, Laura Castañar and Teodor Parella, Magn. Reson. Chem. 53, 399-426 (2015). DOI: 10.1002/mrc.4266.
6. “Pure shift NMR”, Klaus Zangger, Prog. Nucl. Magn. Reson. Spectrosc. 86–87, 1-20 (2015). DOI: 10.1016/j.pnmrs.2015.02.002.

10:00 AM


Fast NMR: Solving a puzzle with most of the parts missing

Prof. Vladislav Y. Orekhov,

University of Gothenburg

    [ abstract ]

30 min


Session 2
  (11:50 am – 1:10 pm EST)

11:10 AM


Intrinsically disordered proteins by NMR: What can ^13C direct detection can tell us?

Prof. Isabella C. Felli,

University of Florence

    [ abstract ]

11:50 AM


Integrative modelling of biomolecular complexes

Prof. Alexandre Bonvin,

Utrecht University

    [ abstract ]

We have developed for this purpose a versatile information-driven docking approach HADDOCK (, accessible through a user-friendly web portal at HADDOCK can integrate information derived from biochemical, biophysical or bioinformatics methods to enhance sampling, scoring, or both. The information that can be integrated is quite diverse: interface restraints from NMR, mutagenesis experiments, or bioinformatics predictions; shape data from small-angle X-ray scattering and cryo-electron microscopy experiments. In my talk, I will introduce HADDOCK and illustrate its capabilities with various examples including some recent work on the use of shape information to guide the docking of both macromolecular and small molecule complexes.

12:30 PM


High molecular-weight complexes in the regulation of gene expression: A view by integrative structural biology

Prof. Teresa Carlomagno,

Leibniz University of Hannover

    [ abstract ]


1. D’Arcy S., Luger K. Curr Opin Struct Biol, 21(6), 728–734 (2011).

2. Fillingham J., Recht J., Greenblatt JF. Mol Cell Biol. 28, 4342–4353 (2008).

3. Driscoll R., Hudson A., Jackson SP. Science, 315, 649–652 (2007).

4. Danilenko N., Lercher L., Gabel F., Kirkpatrick J., Carlomagno T. Nature Commun.10, Article number: 3435 (2019)

50 min


Session 3
  (2:00 – 4:00 pm)

2:00 PM


Mechanochemical Synthesis of Active Pharmaceutical Ingredients and their Characterization with New NMR Crystallographic Methods based on Solid-State NMR of Quadrupolar Nuclei

Prof. Robert W. Schurko,

National High Magnetic Field Laboratory

    [ abstract ]

2:40 PM


Deuterium Metabolic Imaging (DMI), a novel MR-based method to map metabolism in 3D

Prof. Robin A. de Graaf,

Yale University

    [ abstract ]

3:20 PM


How Quantitative NMR Enables New Metabolomics Methods

Prof. Daniel Raftery,

University of Washington

    [ abstract ]

20 min


Session 4
  (4:20 – 5:40 pm)

4:20 PM


Accelerated Identification of Natural Products using Small Molecule Accurate Recognition Technology (SMART) 2.1

Prof. William Gerwick,

University of California, San Diego

    [ abstract ]

5:00 PM


Discovery and characterization of active small molecule ligands targeting the function of ubiquitin specific protease USP7 by a catalytic site independent mechanism

Prof. Till Maurer,

Merck & Co.

    [ abstract ]

Using ligand-based NMR in an activity agnostic fragment-based lead identification (FBLD) effort (5), we have identified small molecule binders to several novel binding sites in USP7. Guided by NMR, protein-ligand complex X-ray structures and biochemical assays, several fragment classes were structurally characterized and chemically modified to bind USP7 with increased affinity and activity. Binders to unique site in the “”palm”” of USP7, the Ubiquitin binding region, were shown to be active in a biochemical and cellular context.

The palm series are of mechanistic interest as they imply a very distinct mechanism of action independent of the catalytic triad by binding in a region that is directly involved in USP7-Ubiquitin interaction. The palm fragments bind USP7 in a site near Asp 305 and Glu 308, residues whose side chains are involved in polar interactions with the side chain of Lys 48 in Ubiquitin present in the Ubiquitin complex crystal structure 1NBF (6). These results suggest a possible mechanism for both steric interference of Ubiquitin binding but also the means by which USP7 recognizes K48 linkages.

I will show using biophysical and biochemical methods as well as cellular assays the relevance of the identified ligands and their binding site and support the postulated mechanism of action with information of their effects on the interaction of USP7 with mono- and di-Ubiquitin.

1 Ray-Coquard, I. et al. Effect of the MDM2 antagonist RG7112 on the P53 pathway in patients with MDM2-amplified, well-differentiated or dedifferentiated liposarcoma: an exploratory proof-of-mechanism study. The lancet oncology (2012). doi:10.1016/S1470-2045(12)70474-6.
2 Colland, F. et al. Small-molecule inhibitor of USP7/HAUSP ubiquitin protease stabilizes and activates p53 in cells. Molecular Cancer Therapeutics 8, 2286–2295 (2009).
3 Brown, C. J., Lain, S., Verma, C. S., Fersht, A. R. & Lane, D. P. Awakening guardian angels: drugging the p53 pathway. Nature Reviews Cancer 9, 862–873 (2009).
4 Nicholson, B. & Suresh Kumar, K. G. The multifaceted roles of USP7: new therapeutic opportunities. Cell Biochem Biophys 60, 61–68 (2011).
5 Methods Enzymol. Vol. 493 (2011)
6 Hu, M. et al. Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde. Cell 111, 1041–1054 (2002).

5:40 PM


NMR-based screening of combinatorial libraries to target protein-protein interactions with reversible or covalent agents

Prof. Maurizio Pellecchia, Ph.D.,

University of California, Riverside

    [ abstract ]

(1) Covalent Inhibitors of Protein-Protein Interactions Targeting Lysine, Tyrosine, or Histidine Residues. Gambini L, Baggio C, Udompholkul P, Jossart J, Salem AF, Perry JJP, Pellecchia M. J Med Chem. 2019 Jun 13;62(11):5616-5627
(2) Aryl-fluorosulfate-based Lysine Covalent Pan-Inhibitors of Apoptosis Protein (IAP) Antagonists with Cellular Efficacy. Baggio C, Udompholkul P, Gambini L, Salem AF, Jossart J, Perry JJP, Pellecchia M. J Med Chem. 2019 Oct 8. doi: 10.1021/acs.jmedchem.9b01108

6:40 PM