North Jersey Section
American Chemical Society

NMR Spectroscopy Topical Group Meetings

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Oct 23, 2013 – NMR Topical Group Meeting

The North Jersey ACS NMR Topical Group proudly presents its October monthly meeting at Rutgers CABM on Wednesday, October 23, 2013

VENUE: Our meetings this year are at the CABM (Center for Advanced Biotechnology and Medicine) on the Rutgers Busch Campus, 679 Hoes Lane West, Piscataway NJ 08854 [ map & directions ].

The meeting is in Room 010, which is located near the main entrance of CABM. Parking will be available in the lot across the street from the CABM building. Dinner will be served in the meeting room.

This meeting is sponsored by Bruker BioSpin

Bruker

Featured Speakers

Talk I

“General Overview of New Products For 2013”

George Anastasi,
Regional sales manager of Bruker BioSpin, Inc.

Talk II

“Recent advances in NMR spectroscopy of encapsulated proteins & nucleic acids dissolved in low viscosity fluids”

Prof. Josh Wand,
Johnson Research Foundation and Department of Biochemistry & Biophysics, University of Pennsylvania Perelman School of Medicine, Philadelphia

Program

    6:00 pm Dinner
    7:00 pm Seminar

Meeting Venue

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

Dinner cost: No charge thanks to the generous sponsorship by Bruker BioSpin.

Doubled Door Prizes!
(4 door prizes for # of attendees < 20, 6 door prizes for # of attendees > 20)

Register: Online below or via e-mail to Swapna Gurla at gvts@cabm.rutgers.edu.

Abstract for Talk II:

Solution NMR spectroscopy is a powerful technique to study protein structure and dynamics on multiple timescales and in many contexts. Sample preparation is often the key ingredient that enables otherwise very difficult studies of complex macromolecular systems. Some time ago we introduced the idea of using solutions of proteins encapsulated within the protective aqueous core of a reverse or inverted micelle and dissolved in low viscosity fluids as a means to overcome the “slow tumbling” problem presented by large, soluble proteins. Since then several advantageous properties of the reverse micelle particle have been used to promote studies of integral and anchored membrane proteins, soluble proteins and nucleic acids of marginal stability as well as investigations of various aspects of protein biophysics such as cold denaturation, protein hydration and protein motion.

Despite this, the approach has not been generally adopted by the NMR community. To make this reverse micelle encapsulation approach more accessible, we have developed an optimized reverse micelle surfactant system. Comprised of the nonionic 1-decanoyl-rac-glycerol and the zwitterionic lauryldimethylamine-N-oxide (10MAG/LDAO), this mixture is found to faithfully encapsulate a diverse set of proteins ranging up to 80 kDa in size and having a broad spectrum of electrostatic properties. Extensive chemical shift analyses indicate that encapsulation conditions that maintain high structural fidelity can be directly found. A clear advantage of 10MAG/LDAO is the active decrease of molecular reorientation time for encapsulated macromolecules larger than ˜20 kDa leading to improved signal-to-noise.

The properties of 10MAG/LDAO are also found to be very favorable for solution NMR studies of lipidated proteins. New and efficient strategies for optimization of encapsulation conditions have also been developed. 10MAG/LDAO performs well in both the low viscosity pentane and ultra-low viscosity liquid ethane and should serve as a general platform for initiating solution NMR studies of proteins and nucleic acids. In a parallel effort, it has been realized that reverse micelle solutions potentially offer a route to implement dynamic nuclear polarization enhancement of protein resonances by avoiding the dielectric heating generally associated with standard aqueous samples. Initial results will be presented. Supported by NSF and the NIH.

 

2013-10-23

(Past Events)

Oct 2, 2013 – NMR Fall Symposium

The North Jersey ACS NMR Topical Group proudly presents its October 2013 Symposium at Rutgers Waksman Institute on the Busch Campus in Piscataway on Wednesday, October 2, 2013 [ register ]

Venue:  Waksman Auditorium

In the building adjacent to
CABM (Center for Advanced Biotechnology and Medicine)
Rutgers University, Busch Campus
679 Hoes Lane West
Piscataway, NJ 08854

Free parking across the street in unreserved spots

NMR 2013 Fall Symposium

This program information is also available as a [ flyer ]. Please take a copy and circulate it among your colleagues.

Note there is a $10 registration fee, which we encourage you pay online below (you don’t need a PayPal account!) but it can be paid at the door. Attendance is free for students, retirees, and unemployed. Pre-registration is required to get a head count.

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2013-10-02

(Past Events)

Jun 12, 2013 – NMR Topical Group Meeting

The North Jersey ACS NMR Topical Group proudly presents its June meeting of 2013 at Rutgers CABM on Wednesday, June 12, 2013[ register ]

NOTE: NEW VENUE: We had been meeting at the Fuji Restaurant, which closed. We've moved our series instead to the CABM (Center for Advanced Biotechnology and Medicine) on the Rutgers Busch Campus, 679 Hoes Lane West, Piscataway NJ 08854 [ map & directions ].

The meeting is in Room 010, which is located near the main entrance of the CABM. Parking will be available in the lot across the street from the CABM building. Dinner will be served in the meeting room.

This meeting is sponsored by

Nexonomics

Featured Speakers

Talk I

19F NMR as a Direct Probe of Intermolecular Interactions by Non-Structural Protein 1 from Influenza A Virus

James M. Aramini, PhD,

Research Assistant Professor, Center for Advanced Biotechnology and Medicine, Rutgers University, Piscataway, NJ

Talk II

“Nexomics Biosciences”

Gregory Kornhaber, PhD,
Nexomics Biosciences, North Brunswick, NJ

Program

    6:00 pm Dinner
    7:00 pm Seminar

Meeting Venue

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

Dinner cost: $12 (no charge for students / postdoc / retired / unemployed)

This event is subsidized by Nexomics Biosciences, which is a New Jersey based Contract Research Organization (CRO) specializing in protein sample and structure determination services.

No charge for seminar only.

Doubled Door Prizes!
(4 door prizes for # of attendees < 20, 6 door prizes for # of attendees > 20)

Register: Online below or via e-mail to Swapna Gurla at gvts@cabm.rutgers.edu.

Abstract for Talk I:

Non-structural protein 1 of influenza A virus, NS1A, is a key multifunctional virulence factor produced in the infected host cell that plays a critical role in evading the host antiviral response. This highly conserved hub protein in influenza infection is comprised of two domains: an N-terminal double-stranded RNA-binding domain (RBD) and a C-terminal effector domain (ED) which binds to a plethora of host cellular proteins. Isolated RBD and ED domains of NS1A both exist as homodimers in solution.

Since the 1960s, 19F has been recognized as a valuable NMR probe for biological systems due to its numerous favorable NMR properties, including its nuclear spin (I = ½), high natural abundance (100%), extremely high sensitivity, wide chemical shift range, minimal inherent background 19F signals, and the exquisite sensitivity of its chemical shift to changes in local environment.

Here we have applied 19F NMR to the study of NS1A from influenza A/Udorn/307/1972 (H3N2) virus. We incorporated 5-fluorotryptophan (5-F-Trp) into NS1A RBD, NS1A ED, and full-length NS1A, and assigned the 19F signals corresponding to the four Trp residues in this protein by site directed mutagenesis. We demonstrate that the 19F signal for W187, located in a functionally important helix-helix interface, can be used to monitor the oligomerization state of the ED (i.e., dimer to monomer transitions). Our 19F NMR data provide strong evidence in favor of conformational exchange at this critical interface in solution. Moreover, for full-length NS1A, 19F NMR provides the first direct spectroscopic evidence that W187, which is known to mediate intermolecular ED:ED interactions in the oligomerization of full-length NS1A, becomes solvent-exposed at protein concentrations below aggregation (ca. 50 %mu;M). Finally, we demonstrate that 5-F-Trp and 4-fluorophenylalanine (4-F-Phe) incorporation combined with 19F NMR serves as a sensitive approach for monitoring the binding of the F2F3 peptide from CPSF30 to NS1A ED.

This work was supported by grants from the NIGMS Protein Structure Initiative U54-GM094597 (to G.T.M.), NIH U01-AI074497 (to G.T.M. and R.M.K.), and NIH R01-AI11772 (to R.M.K.).

 

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2013-06-12

(Past Events)

May 15, 2013 – NMR Topical Group Meeting

The North Jersey ACS NMR Topical Group proudly presents its May meeting of 2013 at the Fuji Japanese Sushi & Seafood  Rutgers CABM on Wednesday, May 15, 2013[ register ]

NOTE: CHANGE OF VENUE: The Fuji Restaurant is closed. This meeting will take place instead at the CABM (Center for Advanced Biotechnology and Medicine) on the Rutgers Busch Campus, 679 Hoes Lane West, Piscataway NJ 08854 [ map & directions ].

The meeting is in Room 010, which is located near the main entrance of the CABM. Parking will be available in the lot across the street from the CABM building. Dinner will be served in the meeting room provided by a RU caterer. Also, we have permission to serve wine.

This meeting is sponsored by
Agilent Technologies

Featured Speakers

Talk I

“Mapping the Energy Landscape of Protein Function using NMR and Calorimetry”

Dr. Tony Mittermaier
Associate Professor
Department of Chemistry, McGill University
Montreal, Canada

Talk II

“Agilent Update and the News from the ENC”

Bill Marathias
NMR Applications Scientist
Agilent Technologies, Inc.

Program

    6:00 pm Dinner
    7:00 pm Seminar

Meeting Venue

Dinner cost: No charge, thanks to sponsorship by Agilent Technologies.

Register: Online below or via e-mail to Swapna Gurla at gvts@cabm.rutgers.edu.

Abstract for Talk I:

Biological macromolecules are inherently dynamic and in many cases depend on changes in conformation and flexibility to perform their physiological roles. In order to understand how they function at an atomic level, it is necessary to map the energetic interactions that govern their structures and dynamics. NMR spectroscopy is well suited to addressing this problem, since it can provide detailed information on molecular conformation and internal motions. Many NMR measurements can be interpreted quantitatively in terms of exchange rates or thermodynamic differences between conformational states, such as folded and unfolded or ligand-free and ligand-bound forms. In this regard, biological NMR data are highly complementary to those of biocalorimetry, for example isothermal titration calorimetry (ITC) and differential scanning calorimetry (DSC). These methods directly detect the heat absorbed and released during protein binding and folding reactions. In fact, the combination of calorimetric and NMR methods provides a clearer picture of molecular processes than does either technique alone. Microcalorimetry is extremely sensitive to the energetics of conformational transitions and macromolecular interactions. However it can be difficult to relate these measurements to specific changes in molecular structure and flexibility without additional information. Conversely, NMR is sensitive to conformation and dynamics at the level of individual atoms, but thermodynamic information is obtained indirectly. Combining NMR and calorimetric measurements has the potential to improve our understanding of how macromolecular structure, dynamics, energetics and function are related, and to redefine our description of biological systems at the atomic level. I will discuss some recent examples from our lab in which NMR and calorimetry have been applied in concert to study fundamental aspects of protein function including folding, molecular recognition, and allostery. 

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2013-05-15

(Past Events)

Mar 20, 2013 – NMR Topical Group Meeting

The North Jersey ACS NMR Topical Group proudly presents its March meeting at the Fuji Japanese Sushi & Seafood on Wednesday, March 20, 2013[ register ]

Advanced Chemistry Development, Inc

This meeting is sponsored by Advanced Chemistry Development, Inc. (ACD/Labs)

Featured Speakers

Talk I

“ACD/Lab’s Spectrus NMR Workbook: A Toolkit for Pharma’s NMR Spectroscopist”

Dr. Janet Caceres-Cortes
Principal Scientist, DAS NMR, Bristol-Myers Squibb
Route 206 & Provinceline Road
Princeton, NJ 08543-4000

Talk II

“Current Developments at ACD/Labs in Tools to Assist the NMR Spectroscopist”

Patrick Wheeler
Product Manager – NMR, Advanced Chemistry Development, Inc.
8 King Street East, Suite 107
Toronto, ON Canada M5C 1B5

Program

    6:00 pm Dinner
    7:00 pm Seminar

Meeting Venue

Dinner cost: No charge, thanks to donation by ACD/Labs.

Register: Online below or via e-mail to Swapna Gurla at gvts@cabm.rutgers.edu.

Abstract for Talk I:

The potential role of metabolites in drug efficacy and safety underscores the importance of detecting and characterizing drug metabolites notwithstanding the often complex metabolic profiles and generation of numerous metabolites of varying concentrations from the drugs of interest. Thus, metabolite identification (ID) studies are an integral part of pre-clinical and clinical drug development activities and in many instances rely on Nuclear Magnetic Resonance (NMR) spectroscopy.

ACD/NMR Workbook provides an array of tools allowing processing of 1D and 2D data. It allows the NMR spectroscopist to perform structure elucidation and identify metabolite modification sites while recording their spectral assignments. A useful practice in metabolite ID is to compare the structural information attained through the analysis of chemical shifts, coupling constants, peak integrations and correlations for the isolated metabolite with those of the parent compound. This is not always a facile endeavor since the quality of the metabolite NMR spectra can be challenged by sensitivity, dynamic range, and matrix interferences. ACD/NMR Workbook has a number of features that facilitate this comparison. This presentation will highlight the new and enhanced features of Spectrus/NMR Workbook over ACD12/Workbook and its utility for metabolite ID and structure elucidation.

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2013-03-20

(Past Events)

Feb 20, 2013 – NMR Topical Group Meeting

The North Jersey ACS NMR Topical Group proudly presents its February meeting at the Fuji Japanese Sushi & Seafood on Wednesday, February 20, 2013.

Featured Speaker

Dr. Nate Traaseth
Assistant Professor, Department of Chemistry, New York University

“Structural Studies of Small Multidrug Resistance Membrane Proteins by Oriented and Magic-Angle-Spinning Solid-State NMR Spectroscopy in Lipid Bilayers”

Register online here or via e-mail to Swapna Gurla at gvts@cabm.rutgers.edu.

Meeting Venue

Fuji Japanese Sushi & Seafood
1345 US Rt 1, North Brunswick, NJ 08902
Please note that Pathmark is no more.
Fuji is on US 1 Southbound.
[ Directions ]

6:00 pm Dinner
7:00 pm Seminar

Dinner cost: $15 ($5 for student, postdoc or retired). No charge for seminar only.

Abstract:

Multidrug resistance (MDR) is a pervasive clinical problem that reduces the effectiveness of treatment against bacterial infections, viral infections, and cancer. Efflux of drugs across the lipid bilayer by MDR membrane protein transporters is one way in which resistance is conferred to the host organism or cell. To derive a structure/function relationship for this class of proteins, our study uses the small multidrug resistance (SMR) family as a model system for deciphering the mechanism of transport with the long-term goal of decoding the evolutionary importance of the transporter family. We used solid-state NMR (SSNMR) spectroscopy to study the topology and structure of EmrE in liposomes (magic-angle-spinning or MAS) and magnetically aligned lipid bilayers (oriented SSNMR or O-SSNMR). The MAS experiments were used to map chemical shift perturbations upon drug binding while the O-SSNMR experiments revealed the change in helix orientation upon binding and transport. Together these complementary techniques showed that drug binding perturbs both the structure of EmrE as well as the helical orientations with respect to the lipid bilayer.

2013-02-20

(Past Events)

Jan 16, 2013 – NMR Topical Group Meeting

The North Jersey ACS NMR Topical Group proudly presented its January meeting at the Fuji Japanese Sushi & Seafood on Wednesday, January 16, 2013.

Featured Speaker

Dr. Charalampos (Babis) Kalodimos
Professor, Department of Chemistry & Chemical Biology, Rutgers University, Piscataway NJ

“NMR of Large Proteins”

Meeting Venue

Fuji Japanese Sushi & Seafood
1345 US Rt 1, North Brunswick, NJ 08902
Please note that Pathmark is no more. Fuji is on US 1 Southbound.
(Directions: http://www.fujiseafoodbuffet.com/directions.php)

6:00 pm Dinner
7:00 pm Seminar

Dinner cost: $15 ($5 for student/postdoc/retired). No charge for seminar only.

Register online here or via e-mail to Swapna Gurla at gvts@cabm.rutgers.edu.

2013-01-16

(Past Events)

Nov 14, 2012 – NMR Topical Group Meeting

The North Jersey ACS NMR Topical Group proudly presented its November meeting at the Fuji Japanese Sushi & Seafood on Wednesday, November 14, 2012.

Featured Speaker

Dr. Roberto R. Gil
Research Professor, Department of Chemistry, Carnegie Mellon University, Pittsburgh, PA

“Structural Analysis of Small Organic Molecules Assisted by Residual Dipolar Couplings”

Meeting Venue

Fuji Japanese Sushi & Seafood
1345 US Rt 1, North Brunswick, NJ 08902
Please note that Pathmark is no more. Fuji is on US 1 Southbound.
(Directions: http://www.fujiseafoodbuffet.com/directions.php)

6:00 pm Dinner
7:00 pm Seminar

Dinner cost: $15 ($5 for student/postdoc/retired). No charge for seminar only.

Registration is now closed.    If you need more information or have questions, please contact Charles Pathirana at Charles.pathirana@bms.com

Abstract

The 2D structure of most small molecules can be in principle straightforwardly determined by manual or automatic analysis of a set of experimental data that includes the molecular formula, a series of 1D and 2D NMR experiments providing through-bond connectivity (COSY, TOCSY, HSQC, HMBC and ADEQUATE/INADEQUATE based experiments), and chemical shift predictions.

This is the main concept embedded in automatic structure elucidation programs. Once the 2D structure is available, the determination of the relative spatial arrangement (configuration and preferred conformation) of all atoms in the molecule is a more challenging task that it is commonly addressed in NMR by using NOE and 3J coupling constants analysis, as well as recent developments on the application of DFT calculation of 13C chemical shifts.

However, it is difficult to assess how many samples are sitting on the laboratory’s refrigerators waiting for an independent methodology that could lift some of the ambiguities generated by the use of conventional NMR methods. The development of the application of Residual Dipolar Couplings (RDCs) to the configurational and conformational analysis of small molecules has matured enough in the recent years to perform this task in an almost straightforward way, without even the need of using NOE and 3J coupling analysis, as it will be presented here for the analysis of rigid and semi-rigid small molecules.

The application of RDCs to the analysis of flexible molecules is still a field of research with plenty of room for development and a generally accepted approach is not available yet.

2012-11-14

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