[raw] The North Jersey ACS NMR Topical Group is pleased to presents its 2020 Fall Symposium online on Tues, Oct 20, 2020, 8:00 am – 6:00 pm EST

North Jersey ACS NMR Topical Group

presents the

2020 Virtual NMR Symposium

October 20th, 2020

Link to webex: https://www.njacs.org/nmr-symposium-webex

Password: NJACS-2020

Attendance is FREE of charge

[ flyer | Keynote Address ]


2020 Virtual NMR Symposium

Session 1
  (8:00 – 10:50 am EST)

– Chair: István Pelczer, Princeton University

8:00 am

Justyna Sikorska

Opening remarks

Justyna Sikorska,


NJACS NMR Topical Group

8:10 am

Yulan Wang


Detection of metabolic reprogramming associated with HBV infection using metabonomics

Yulan Wang,

Singapore Phenome Center

    [ abstract ]

8:50 am

Ruth Gschwind


NMR As Mechanistic Tool In Photocatalysis

Ruth M. Gschwind,

University of Regensburg

    [ abstract ]

9:30 am

Gareth Morris


Ultraclean pure shift NMR?

Gareth Morris,

University of Manchester

    [ abstract ]

10:10 am

Vladislav Orekhov


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

Vladislav Y. Orekhov,

University of Gothenburg

    [ abstract ]

10:50 am

Break (20 min)

Session 2
  (11:10 am – 12:10 pm EST)

– Chair: Gaetano T. Montelione, RPI

11:10 am

Isabella Felli


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

Isabella C. Felli,

University of Florence

    [ abstract ]

11:50 am

Alexandre Bonvin


Integrative modelling of biomolecular complexes

Alexandre Bonvin,

Utrecht University

    [ abstract ]

12:30 pm

Teresa Carlomagno


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

Teresa Carlomagno,

Leibniz University of Hannover

    [ abstract ]

1:10 pm

Break (50 min)

Session 3
  (2:00 – 4:00 pm EST)

– Chair: Mark McCoy, Merck & Co.

2:00 pm

Robert Schurko


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

Robert W. Schurko,

National High Magnetic Field Laboratory

    [ abstract ]

2:40 pm

Robin de


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

Robin A. de Graaf,

Yale University

    [ abstract ]

3:20 pm

Daniel Raftery


How Quantitative NMR Enables New Metabolomics Methods

Daniel Raftery,

University of Washington

    [ abstract ]

4:00 pm

Break (20 min)

Session 4
  (4:20 – 7:00 pm EST)

– Chair: Luciano Mueller, Bristol-Myers Squibb

4:20 pm

Bill Gerwick


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

William Gerwick,

University of California, San Diego

    [ abstract ]

5:00 pm

Till Maurer


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

Till Maurer,

Merck & Co.

    [ abstract ]

5:40 pm

Maurizio Pellecchia


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

Maurizio Pellecchia,

University of California, Riverside

[ abstract | slides ]

We demonstrated that screening of combinatorial libraries using biophysical approaches including NMR spectroscopy (HTS by NMR) can identify suitable initial binding agents targeting protein-protein interactions (PPIs). The optimization of such agents into potent and selective compounds, however, remains a challenging task. In one example I will report that NMR-guided, structure-based optimizations can mature initial hit molecules into potent putative drug candidates. Nowadays, approaches that are aimed at designing targeted covalent inhibitors, that is drugs that bind irreversibly with their targets, are heavily pursued by academia, biotech, and pharmaceutical companies. These approaches have culminated in the recent approval of several covalent drugs in oncology. These drugs most often target the natural amino acid cysteine that is more reactive that all other amino acids in a protein target. I will report on several recent studies from the laboratory aimed at deriving derive potent, selective, cell permeable and efficacious, protein-protein interactions (PPIs) antagonists by designing agents that can react with lysine, tyrosine, or histidine residues that are ubiquitously present at binding interfaces of PPIs. With the resurgence and the success of covalent drugs, and the paucity of effective PPIs antagonists in the clinic, it is obvious that these studies provide novel and practical insights into the optimization and derivation of effective covalent agents that widen the available target space beyond Cysteine, to include other more abundant residues such as lysine, tyrosine, or histidine. Examples will include potent and selective Lys-covalent agents targeting apoptotic proteins in the IAP and Bcl-2 proteins.
(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

Bradley Falk


Closing remarks

Bradley Falk,


NJACS NMR Topical Group

7:00 pm


[/raw] [raw]

We acknowledge the generous support of our sponsors:


Oxford Instruments    

Nexomics Biosciences    

Suraj Manrao Science Fund    

Luciano Mueller    



Wilmad LabGlass    


  Cambridge Isotope Laboratories    

Magritek, Ltd    

Millipore Sigma    

ACD Labs    

New Era