North Jersey Section
American Chemical Society

NMR Spectroscopy Topical Group Meetings

back

Older Events

Jan 20, 2016 – NMR Topical Group Meeting

The North Jersey ACS NMR Topical Group proudly presents its January monthly meeting at Princeton University, Frick Chemistry Laboratory Atrium, Wednesday, January 20, 2016. [ register ]

Featured Presentation

Prof. Rob Messinger

Department of Chemical Engineering, The City College of New York

“Measuring and Understanding Local (Dis)order: Crystallization of Zeolite Nanosheets & Defects in Li-ion Battery Electrodes”

Abstract:

Measuring and understanding how order develops in crystallizing materials is a challenging problem, especially during the syntheses of self-assembled materials that exhibit both crystalline and mesoscopic order. Surfactant-directed zeolite MFI nanosheets exhibit improved transport and catalytic properties compared to their bulk zeolite counterparts, particularly with respect to large molecules. During their hydrothermal syntheses, coupled framework crystallization and surfactant self-assembly processes occur that are poorly understood and difficult to control. Local compositions, atomic and mesoscale structures, and surfactant-framework interactions were monitored throughout their syntheses by multi-dimensional solid-state 1H and 29Si nuclear magnetic resonance (NMR) spectroscopy, X-ray diffraction (XRD), and electron microscopy measurements. The analyses establish how the atomic and mesoscale framework structures evolve during hydrothermal synthesis, revealing that the zeolite MFI nanosheets form via intermediate nano-layered frameworks with 2D crystal-like structures.

Similarly, identifying and characterizing atomic-scale disorder in crystalline solids can be challenging experimentally, particularly for lithium-ion intercalation electrodes that can exhibit multiple oxidation and spin states. LiVPO4F is one of the most energy-dense polyanionic electrode materials currently known for lithium-ion batteries, but recent solid-state NMR measurements have revealed unusual extents of local disorder. Highly crystalline LiVPO4F samples were synthesized, as determined by XRD and scanning transmission electron microscopy (STEM) measurements. Solid-state 7Li NMR spectra reveal unexpected paramagnetic lithium environments that can account for up to 20% of the total lithium content. Multi-dimensional and site-selective solid-state 7Li-7Li dipolar recoupling NMR experiments establish unambiguously that the unexpected lithium environments are defects within the LiVPO4F crystal structure, further revealing the sub-nanometer-scale proximities between them. The lithium defects are shown to exhibit altered electronic environments that result from changed oxidation states of nearby paramagnetic vanadium atoms. The results provide a general strategy for characterizing sub-nanometer-scale disorder in lithium-containing crystalline solids, including highly paramagnetic materials with short NMR relaxation times on the order of ms.

Program

6:00 pm   Dinner
7:00 pm  Seminar

Meeting Venue

A57, Frick Chemistry Laboratory Atrium, Princeton University [ directions ]

Dinner Cost:

$15 employed / $5 students, postdoc, retired, unemployed.
No charge for seminar only.

Questions:

Frank.Rinaldi@bms.com or Anuji.Abraham@bms.com

Register:

Please register online below or via e-mail to Frank Rinaldi   frank.rinaldi@bms.com    Anuji Abraham Anuji.Abraham@bms.com

2016-01-20

(Past Events)

Oct 21, 2015 – NMR Symposium

4th Annual NMR Symposium


The North Jersey ACS NMR Topical Group and Princeton ACS Section present the 4th Annual NMR Symposium.

Date:. Wednesday, October 21, 2015
Place: Princeton University

Note: Registration for the free admission events is encouraged to help with planning. Registration for dinner is required and closes on October 16th. Register online or by emailing galiadeb@gmail.com

[ registersponsors | directions | NMR homepage ]

Speakers

Mei Hong

Mei Hong

Robert Powers

Robert Powers

Hashim Al-Hashimi

Hashim Al-Hashimi

Mark McCoy

Mark McCoy

Kevin Gardner

Kevin Gardner

Peter Caravan

Peter Caravan

Program

Afternoon session – McDonnell Hall A01 – free admission

1:00 - 1:45 pm – Mei Hong

Massachusetts Institute of Technology

“Solid-State NMR Investigations of the Structure, Dynamics and Mechanisms of Viral Membrane Proteins”

1:45 - 2:30 pm – Robert Powers

University of Nebraska-Lincoln

“Metabolomics and Drug Discovery”

2:30 - 3:15 pm – Hashim Al-Hashimi

Duke University

“Hoogsteen Base Pairs in Duplex DNA: More Sleepless Nights for Watson”

3:15 - 3:45 pm – Coffee break

3:45 - 4:30 pm – Mark McCoy

Merck Research Labs

“BioNMR Applications in Cancer Drug Discovery and Development”

4:30 - 5:15 pm – Kevin Gardner

City University of New York

“Environmentally-Controlled Protein/Protein Interactions:  Nature’s Switches, Scientists’ Tools”

5:30 - 6:30 pm – Social mixer – Frick Chemistry Atrium, free admission

Evening session – Frick Taylor Auditorium – free admission – Sponsored by Princeton ACS

6:30 - 7:30 pm – Peter Caravan

MGH/Harvard, Boston

“Molecular Magnetic Resonance Imaging”

7:30 - 8:30 pm – Dinner – Frick Chemistry Atrium - $20 per person – pay at the door - register


Directions

The opening session of the Symposium is at

McDonnell Hall A01,
Princeton NJ 08540

on the campus of Princeton University. Parts of the event will be held in the adjacent Frick Chemistry Hall[ Campus Map | Google Map ]

Parking: Public parking is available in Lot 21.  (See Campus Map — Lot 21 is east of Frick and McDonnell Halls).

McDonnell Hall: Take the Jadwin entrance on Stadium Drive (see campus map). We will post signs to the location of the seminar room.

Public transportation: It is possible to take NJ Transit all the way to Princeton campus (the symposium location is ~ 10 min walk from the train station). Take the Northeast Corridor NJ transit train to Princeton Junction, then transfer to the small “dinky” train that ends on campus (5 min train ride). For assistance, email galiadeb@gmail.com.

top

We are very grateful to our sponsors
Luciano Mueller BMS Bruker Biospin JEOL Cambridge Isotope Laboratories Sigma-Aldrich Wilmad-LabGlass New Era Nexomics Biosciences Suraj Manrao Science Fund MestreLab Research Magritek ACD Labs Icon Isotopes / Berry & Associates

top






 

top

2015-10-21

(Past Events)

September 30, 2015 – NMR Topical Group Meeting

The North Jersey ACS NMR Topical Group proudly presents its September monthly meeting at Rutgers University, Busch Campus,
CABM, Room 010 (Center for Advanced Biotechnology and Medicine)
679 Hoes Lane West, Piscataway NJ 08854
Wednesday, September 30, 2015. [ register ]

Abstract

Recent developments in solid state probe technology have allowed for previously unrealized rotational rates up to 111 kHz. This fast spinning rate allows for a plethora of new types of experiments in solid-state NMR.  Under “fast mas” conditions, both increased 13C coherence lifetimes and proton detection experiments open new gateways to study the biological solids as well as materials and pharmaceutical sciences.  In combination with semi-automated acquisition software, SSNMR has never been more easily implemented.

Times

6:00 pm   Dinner
7:00 pm  Seminar

Venue

Rutgers University, Busch Campus, CABM, Room 010 (Center for Advanced Biotechnology and Medicine) 679 Hoes Lane West, Piscataway NJ 08854

Dinner Cost:

Free (sponsored by Bruker BioSpin)

Directions to Rutgers University, Busch Campus

Questions: galiad@princeton.edu

Door Prizes!

Register:

Please register online below or via e-mail to Galia Debelouchina at galiadeb@gmail.com.

 

top


2015-09-30

(Past Events)

June 17, 2015 – NMR Topical Group Meeting

The North Jersey ACS NMR Topical Group proudly presents its June monthly meeting at Princeton University, Frick Chemistry Laboratory Atrium, Wednesday, June 17, 2015. [ register ]

Abstract:

The integral membrane protein DsbB in Escherichia coli is responsible for oxidizing the periplasmic protein DsbA, which forms disulfide bonds in substrate proteins. We have developed a high-resolution structural model by combining experimental X-ray and solid-state NMR with molecular dynamics (MD) simulations. We embedded the high-resolution DsbB structure, derived from the joint calculation with X-ray reflections and solid-state NMR restraints, into the lipid bilayer and performed MD simulations to provide a mechanistic view of DsbB function in the membrane. Further, we revealed the membrane topology of DsbB by selective proton spin diffusion experiments, which directly probe the correlations of DsbB with water and lipid acyl chains. NMR data also support the model of a flexible periplasmic loop and an interhelical hydrogen bond between Glu26 and Tyr153. Significant sensitivity enhancement of membrane protein was achieved using chelator lipids with paramagnetic metal ions, which can be readily incorporated into the existing preparation of membrane samples. These solid-state NMR techniques are transferrable to many membrane-associated protein systems.  

Program

6:00 pm   Dinner
7:00 pm  Seminar
DOOR PRIZES!

Meeting Venue

A57, Frick Chemistry Laboratory Atrium, Princeton University

Dinner Cost:

$15 employed / $5 students, postdoc, retired, unemployed.
No charge for seminar only.

Directions to Frick Chemistry Laboratory

Questions: galiad@princeton.edu

Register:

Please register online below or via e-mail to Galia Debelouchina at galiadeb@gmail.com.

 

top


2015-06-17

(Past Events)

May 20, 2015 – NMR Topical Group Meeting

The North Jersey ACS NMR Topical Group proudly presents its May monthly meeting at Rutgers University Busch Campus on Wednesday, May 20, 2015. [ register ]

Abstract:

Nanoparticles have been used industrially for a variety of applications from drug delivery, coatings to electronic materials. The intricate morphologies built into these nanoparticles and their interactions to surfactants, polymers and other nanoparticles provide unique physical properties that are critical to a variety of industrial applications. In this talk we will discuss some of the selective excitation and detection techniques for solid state (dipolar filters) as well as solution state (diffusion filtered – PFGNMR) to probe these properties. We will also discuss the new mechanistic insight from these NMR techniques into shear thinning viscosity of coatings due to rheology modifier (polymer) interaction to polymeric nanoparticles.

Program

6:00 pm   Dinner
7:00 pm  Seminar
DOOR PRIZES!

Meeting Venue

CABM - Room 010 (Center for Advanced Biotechnology and Medicine)

Rutgers Busch Campus
    679 Hoes Lane West, Piscataway NJ 08854
    Directions: http://rumaps.rutgers.edu/?id=C71942

Dinner Cost:

$15 employed / $5 students, postdoc, retired, unemployed.
No charge for seminar only.

Questions: galiad@princeton.edu

Register:

Please register online below or via e-mail to Galia Debelouchina at galiadeb@gmail.com.

 

top


2015-05-20

(Past Events)

Mar 25, 2015 – NMR Topical Group Meeting

The North Jersey ACS NMR Topical Group proudly presents its February monthly meeting at Rutgers University Busch Campus on Wednesday, March 25, 2015. [ register ]

Program

6:00 pm   Dinner
7:00 pm  Seminar
DOOR PRIZES!

Meeting Venue

CABM - Room 010 (Center for Advanced Biotechnology and Medicine)

Rutgers Busch Campus
    679 Hoes Lane West, Piscataway NJ 08854
    Directions: http://rumaps.rutgers.edu/?id=C71942

Dinner Cost:

$15 employed / $5 students, postdoc, retired, unemployed.
No charge for seminar only.

Questions: galiad@princeton.edu

Register:

Please register online below or via e-mail to Galia Debelouchina at galiadeb@gmail.com.

 

top


2015-03-25

(Past Events)

Feb 18, 2015 – NMR Topical Group Meeting

The North Jersey ACS NMR Topical Group proudly presents its February monthly meeting at Princeton University on Wednesday, Feb 18, 2015. [ register ]

Program

6:00 pm   Dinner
7:00 pm  Seminar
DOOR PRIZES!

Meeting Venue

Frick Chemistry Laboratory, Room A57 (Lobby Level)
Princeton University
Princeton, NJ 08540

Location map: http://m.princeton.edu/map/campus?bldid=0649
Parking: Lot 21, see map.

If you would like to arrive by train, let us know so that we can arrange transportation to campus.

Dinner Cost:

$15 employed / $5 students, postdoc, retired, unemployed.
No charge for seminar only.

Questions: galiad@princeton.edu

Register:

Please register online below or via e-mail to Galia Debelouchina at galiadeb@gmail.com.

Abstract:

Biomacromolecules constitute an important segment of pharmaceuticals and exhibit an increasing percentage in pipelines, and play crucial roles in the drug research and development.  Many categories of pharmaceutically interesting molecules have been comprehensively characterized in my research, including antimicrobial drugs and peptides, antiviral drug for influenza A infection, ion channels and amyloid fibrils, using multidimensional Solid-State NMR (SSNMR). Their chemical and biophysical properties of SSNMR interest include structure, aggregation, drug-water, drug-membrane, and drug-protein interactions. My research goal is to investigate these properties and correlate such valuable structural and dynamic information with their pharmaceutical and biological functions to uncover the underlying mechanisms.

In this talk, I’ll take a few examples to illustrate the role of SSNMR in the characterization of these drugs, membrane-active peptides and ion channels. In particular, I’ll show how 13C, 15N, 19F and 31P NMR can be successfully utilized to characterize many natural abundant drug molecules. Domain interactions studied by 1H spin diffusion and NMR relaxation will also be discussed. These examples will include the antimicrobial mechanism of a drug in clinical trial, inhibition of the replication of influenza A virus, and the mechanism of an antimicrobial peptide that shows double gram selectivity. In addition, resent structural findings of ion channels, i.e. voltage gated ion channels (Kv and VDAC), will be discussed. In these examples, I’ll discuss a few cutting-edge SSNMR techniques including 1H-detection at ultra-fast spinning and signal enhancement by dynamic nuclear polarization (DNP), and their potential impact on drug characterization.

 

top


2015-02-18

(Past Events)

Jan 21, 2015 – NMR Topical Group Meeting

The North Jersey ACS NMR Topical Group proudly presents its January monthly meeting at
Rutgers CABM
on Wednesday, Jan 21, 2015. [ register ]

Program

6:00 pm   Dinner
7:00 pm  Seminar

Meeting Venue

CABM - Room 010 (Center for Advanced Biotechnology and Medicine)

Rutgers Busch Campus
    679 Hoes Lane West, Piscataway NJ 08854
    Directions: http://rumaps.rutgers.edu/?id=C71942

Dinner Cost:

$15 employed / $5 students, postdoc, retired, unemployed. No cost for seminar only.

Register:

Please register online below or via e-mail to Swapna Gurla at gvts@cabm.rutgers.edu.

Abstract:

Though the detection of disease and abnormal pathology by magnetic resonance imaging (MRI) has been aided significantly by the use of gadolinium (Gd3+)-based contrast agents (CAs) over the past three decades, current CAs enhance contrast at a small fraction of what is theoretically possible.  We have investigated increasing per-dose CA efficacy both by control of the Gd3+-inner-sphere water exchange rate and via binding to a macromolecular target.

The Gd3+ chelate of 1,4,7,10-tetraazacyclododecane-1,4,7,10-tetraacetate (DOTA), a clinically-established CA, exists as two interconverting coordination geometries which have varying water exchange rates.  A thorough structural characterization of chelates of a DOTA-derivative which cannot undergo conformational exchange was carried out.  These studies show that a single enantiomer of the ligand (S)-2-(4-nitrobenzyl)-1,4,7,10-tetraazacyclododecane-1,4,7,10-tetra(α-methyl)acetate (NB-DOTMA) can yield chelates which are both diastereoisomeric and regioisomeric.  Molecular mechanics simulations generated from the characterization data indicate that the nitrobenzyl (NB) substituent is oriented in different directions for the two possible regioisomers.

The nuclear magnetic resonance (NMR) spectra of Eu-NB-DOTMA at various temperatures were compared.  Unexpectedly, the chelates showed time-averaged structures which differ with a change in water exchange rate – the faster the rate, the greater the deviation from the expected structure.  Consideration of the structures of Ln3+ chelates without accounting for their dynamic behavior does not yield an accurate value for the time-averaged hydration state. These observations suggest the “optimal” water exchange rate calculated using Solomon-Bloembergen-Morgan (SBM) theory may not lead to the highest-efficacy CAs.

The NB group was chemically converted to confer macromolecular binding capability, and the orientation of the NB substituent may have a significant impact on the binding and/or relaxation behavior of a prototypical CA.  Binding and relaxometric studies of macromolecule-targeting derivatives of Gd-NB-DOTMA both by the author and in another lab showed that the coordination isomer with the slower water exchange rate should lead to more effective contrast, in direct opposition to the prevailing view of water exchange in the MRI community.

top


2015-01-21

(Past Events)

Dec 3, 2014 – NMR Topical Group Meeting

The North Jersey ACS NMR Topical Group proudly presents its December monthly meeting at Rutgers CABM on Wednesday, Dec 3, 2014. [ register ]

Program

    6:00 pm Dinner
    7:00 pm Seminar

Meeting Venue

    CABM – Room 010 (Center for Advanced Biotechnology and Medicine)
    Rutgers Busch Campus
    679 Hoes Lane West, Piscataway NJ 08854
    Directions: http://rumaps.rutgers.edu/?id=C71942

Dinner Cost:

$15 employed / $5 students, postdoc, retired, unemployed. No cost for seminar only.

Register:

Please register online below or via e-mail to Swapna Gurla at gvts@cabm.rutgers.edu.

Abstract:  In an untargeted metabolomic study the search for biomarker molecules serves to answer many questions, for which there is a need to find out the identity of these compounds of interest. Several dozen metabolites are normally detected by NMR analysis of a biofluid in measurable quantities. These spectra can have about a few hundred peaks, including overlapping peaks, variable multiplicities and different peak widths. The identification of compounds is normally done with the aid of commercial software packages containing their own databases, by literature search, and/or by searches in public databases by lists of chemical shifts. 2D NMR spectra also aid, by means of finding correlations to 13C atoms, to other 1H atoms, or by evaluating multiplets in a J-Resolved experiment. Given the amount of data collected for the multivariate data analysis, “statistical correlations” are attainable and are of utmost help to submit a “better” query on a database. The most popularized version so far was published almost a decade ago and named STOCSY, standing for Statistical TOtal Correlation SpectroscopY (Cloarec, O. et al., Anal. Chem., 2005, 77(5), 1282-1289, from Imperial College, UK). It is the statistical analysis of several experiments, not an NMR experiment per se, and it is based on the colinearity of the variations of the intensities of the peaks pertaining to the same compound over the spectra set, due to the changes in composition among the samples. Being “born” as a tool analyzing homo-spectroscopies (correlations of 1H to 1H), it had adaptations and variations that led to correlation analysis for biomarker identification on experiments of different nuclei, diffusion-edited and cross-platform (with mass spectrometry for example), as well as for finding pathway connectivities. It can be applied to 1D and 2D data, as well as to “small size” data matrices like in a “spectrum-to-spreadsheet” procedure (which I like to name Stick-STOCSY). Improvements for information recovery can be obtained by further statistical analysis on the (information redundant) STOCSY data matrix. 13C and 1D projections from 1H 2D J-Resolved spectra proved also to be good experiments to use STOCSY on, as the tool suffers from overlapped peaks that abound in some regions of the standard 1H spectrum of biofluids. Examples of its application on biological samples and synthetic mixtures will be shown (as it is not exclusive to biological samples).

top


2014-12-03

(Past Events)

Oct 22, 2014 – NMR Fall Symposium

NMR Fall Symposium


The North Jersey ACS NMR Topical Group proudly presents its October 2014 Symposium at Rutgers Waksman Institute on the Busch Campus in Piscataway on Wednesday, October 22, 2014[ registersponsors ]

Venue

Waksman Institute Auditorium
In the building adjacent to
CABM (Center for Advanced Biotechnology and Medicine)

Rutgers University, Busch Campus
679 Hoes Lane West
Piscataway, NJ 08854   [ map & directions ]

Free parking across the street in unreserved spots.

Program

1:00 pm - Opening remarks

1:05 pm - Robert Griffin

Massachusetts Institute of Technology

“Amyloid, Membranes, Microwaves and MAS”

1:55 pm - Teresa Fan

University of Kentucky

“Exploring Lung Cancer Metabolome: From Bench to Bedside”

2:45-3:15 pm - Coffee break

3:15 pm - Eric Munson

University of Kentucky

“New Applications of Solid-State NMR to Pharmaceuticals”

4:05 pm - Michael Reily

Bristol-Myers Squibb

“Small molecule NMR in Pharma: Using less, doing it quicker and finding biomarkers”

4:55 pm - Marc Caporini

Bruker BioSpin

“Applications of Solid-State NMR using Dynamic Nuclear Polarization with Improved Sensitivity and Fast Acquisition Times.”

5:45 pm - Closing remarks

6:00 - 7:00 pm - Reception - sponsored by Bruker Biospin (in the CABM lobby)


Sponsors

We are grateful to our sponsors for making this symposium possible!

Primary Sponsors

Bruker Biospin Cambridge Isotope Laboratories Nexomics Biosciences

Additional Sponsors
MestreLab Research Wilmad Glass ACD Labs JEOL
Agilent Technologies New Era Sigma-Aldrich
Suraj Manrao Science Fund Luciano Mueller


top

2014-10-22

Top