North Jersey Section
American Chemical Society

NMR Spectroscopy Topical Group Meetings

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Sep 17, 2014 – NMR Topical Group Meeting

The North Jersey ACS NMR Topical Group proudly presents its September monthly meeting at Rutgers CABM on Wednesday, September 17, 2014. [ register ]

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 is available in the lot across the street from the CABM building. Dinner will be served in the meeting room.

Bruker

Featured Presentations

"Evolving Approaches to Small Molecule Structure Elucidation"

Robert Thomas Williamson, PhD, Merck & Co.

and

"ASSURE-RMS: Applications to Competitive Intelligence, Detection of Adulteration and Quality Control"

Kimberly L. Colson, PhD, Bruker BioSpin

Program

6:00 pm Dinner & wine tasting (Sponsored by Bruker-3-4 door prizes!!!!
Note: Dinner is free but please register below, so we know how many people to expect
7:00 pm Seminar: “Evolving Approaches to Small Molecule Structure Elucidation” By Robert Thomas Williamson, PhD, Merck & Co.
7:30 pm Seminar: “ASSURE-RMS: Applications to Competitive Intelligence, Detection of Adulteration and Quality Control” By Kimberly L. Colson. PhD, Bruker BioSpin

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

Cost: The meeting is free, thanks to the generosity of our sponsor.

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

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2014-09-17

(Past Events)

Jun 18, 2014 – NMR Topical Group Meeting

The North Jersey ACS NMR Topical Group proudly presents its June monthly meeting at Rutgers CABM on Thursday, June 18, 2014. [ register ]


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 is available in the lot across the street from the CABM building. Dinner will be served in the meeting room.

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

Cost: The meeting is free, thanks to the generosity of our sponsor.

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

Abstract: As the pharmaceutical and materials research industries continue to rely on specialty and custom chemical manufacturers to supply chemical building blocks, fragment libraries and novel investigational compounds for screening, a growing body of evidence points to a systematic failure rate of materials supplied. In general, between 2% to 8% of milligram and gram scale quantities of specialty chemicals have been reported to be incorrect. Recently, the pharmaceutical industry has begun turning to a process called Auto Structure Verification (ASV) by NMR. Based on 1H and 13C NMR chemical shift prediction comparisons to experimental data and automated assignment of atoms to spectrum features, ASV aims to protect against the consequences of errors in supply chain ordered compounds and internal custom syntheses. ASV has the potential to identify nearly 70% – 80% of incorrect isomer structures that LCMS cannot. Recent high profile case studies, such as in C&E News, highlighting incorrectly synthesized Bosutinib sold by third party vendors (Bethany Halford , Bosutinib Buyer Beware, C&E News May 21, 2012, p34) for research benchmark purposes, demonstrate the vulnerability of our discovery programs to supply chain induced synthesis errors. ASV may be helpful in preventing future cases.

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2014-06-18

(Past Events)

May 29, 2014 – NMR Topical Group Meeting

The North Jersey ACS NMR Topical Group proudly presents its May monthly meeting at Rutgers CABM on New Date: Thursday, May 29, 2014. [ register ]  Note: This meeting had been scheduled on May 21.

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 is available in the lot across the street from the CABM building. Dinner will be served in the meeting room.

Featured Presentations

I. “Agilent Technology Overview”

Bill Marathias Ph.D.

NMR Applications Scientist, Agilent Technologies, Inc, Boston MA

II. “NMR, Metabolomics, and Fermentation Process Analysis”

D. Christopher Roe

Corporate Center for Analytical Sciences
DuPont Experimental Station, Willmington, DE

Program

6:00 pm Dinner
7:00 pm Presentation by Dr Marathias
7:15 pm Presentation by Dr Roe

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 is free, compliments of our sponsor.

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

Abstract for Talk II:

Fermentation processes constitute a significant aspect of DuPont’s drive to sustainability and the production of renewably sourced materials. Fermentation process analysis typically involves monitoring selected metabolites and products, and although trends may be discerned, it is hard to know how to relate these observations to overall process performance. In an effort to accelerate fermentation process development, multivariate methods are being applied to combined fermentation and analytical data sets in order to provide an overview of the fermentation process. The goal is to identify differentially expressed metabolites that contribute significantly to the differences between fermentations (e.g., growth variability, high vs. low titer, or one strain vs. another). This information can be assessed for biological significance, and metabolic engineering can be considered for the identified metabolic pathways. The merits of NMR for metabolomic analysis will be described along with data “pre-processing” methods prior to multivariate analysis. A synopsis of multivariate methods will be given and examples of fermentation time course studies will be presented.

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2014-05-29

(Past Events)

Apr 16, 2014 – NMR Topical Group Meeting

The North Jersey ACS NMR Topical Group proudly presents its April monthly meeting at Princeton University on Wednesday, April 16, 2014[ register ]

VENUE: Please note the change in location for this meeting.  The meeting will be at Princeton University, with the dinner in the Lobby of Frick Chemistry Building, and the seminar at Jadwin A06 (just across from the Chemistry Building)

Featured Speaker

“Early stages of protein folding and intrinsic disorder explored by NMR and hydrogen exchange”

Heinrich Roder

Fox Chase Cancer Center, Philadelphia, PA 19111

Program

6:00 pm  Dinner
7:00 pm  Seminar

Meeting Venue

NOTE CHANGE IN LOCATION FOR THIS MEETING

Princeton University, Princeton, NJ

Dinner – Lobby of Frick Chemistry Building

Seminar – Jadwin A06 (just across from the Chemistry Building)

Directions: http://m.princeton.edu/map/campus

Parking: Lot 21, see campus map

Dinner cost: $15 employed/ $5 for students, postdocs, retired and unemployed

No charge for seminar only

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

Abstract:

My talk will focus on our recent applications of NMR and hydrogen exchange for exploring early stages of protein folding and intrinsic disorder. By coupling NMR-detected H/D exchange with ultrafast quenched-flow mixing we have been able to obtain residue-specific structural insight into the ensemble of states populated during the initial stages of folding of cytochrome c (Fazelinia, H.; Xu, M.; Cheng, H.; Roder, H. J. Am. Chem. Soc. 2014, 136, 733-40). The pH-dependence of amide protection, combined with direct measurement of intrinsic exchange rates in the unfolded protein, showed that amide protons in three α-helical segments in the C-terminal half of cytochrome c were preferentially protected from solvent exchange within 100 microseconds of initiating the folding reaction while the N-terminal α-helix remained unprotected. Thus, sequence-local helix-helix contacts are formed preferentially during early stages of folding whereas long-range (N- to C-terminal) become important only during the later stages of folding (> 3 ms). These findings provide compelling evidence that specific structural events rather than a general hydrophobic collapse of the protein chain dominate the initial stages of folding. I will also present recent progress in our studies on the dynamic properties and functional role of intrinsically disordered regions in NHERF1, a 358-residue protein containing a pair of PDZ domains and a C-terminal motif separated by long flexible linkers. Structural and dynamic NMR, along with other biophysical methods, are providing detailed insight into the conformational equilibria and binding properties of this signaling adaptor.

2014-04-16

(Past Events)

Feb 19, 2014 – NMR Topical Group Meeting

The North Jersey ACS NMR Topical Group proudly presents its February monthly meeting at Rutgers CABM on Wednesday, February 19, 2014[ register ]

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 is available in the lot across the street from the CABM building. Dinner will be served in the meeting room.

Featured Speaker

“Mapping Protein Folding Landscapes Using High Pressure NMR”

Catherine Royer

Department of Biological Sciences
Rensselaer Polytechnic Institute

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: $15 employed/ $5 for students, postdocs, retired and unemployed

No charge for seminar only.

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

Abstract:

Despite significant progress in recent years in understanding protein structural dynamics we still lack sufficient experimental knowledge of protein folding energy landscapes. Moreover, we cannot predict folding transitions states or routes cheapambienpriceonline.com from amino acid sequence or structure. Nor is it known how sequence encodes the conformational fluctuations and heterogeneity required for protein function in specific contexts. We have recently demonstrated that pressure induced unfolding occurs largely because of specific packing defects or void volumes, in the folded structures of proteins that disappear upon unfolding, leading to a decrease in molar volume. Unlike denaturant or temperature perturbations, the effects of which depend on the amount of exposed surface area in the unfolded states of proteins, pressure effects depend on specific properties of folded states. And because packing defects are local and specific, pressure perturbation acts locally to decrease volume, thus allowing for the characterization of intrinsic folding cooperativity. Pressure also provides access to conformational states inaccessible by other methods. Coupling high pressure with multi-dimensional NMR is particularly powerful, as it provides site specific observables throughout the structure of the protein. Used in steady-state and p-jump mode, high pressure NMR has revealed unexpected complexity in the folding rates and routes of cavity-bearing variants of Staphylococcal nuclease. The results underscore the subtlety of the sequence determinants of folding landscapes.

2014-02-19

(Past Events)

Jan 22, 2014 – NMR Topical Group Meeting

The North Jersey ACS NMR Topical Group proudly presents its January monthly meeting at Rutgers CABM on Wednesday, January 22, 2014[ register ]

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 is available in the lot across the street from the CABM building. Dinner will be served in the meeting room.

Featured Speaker

“Unraveling the Structural Organization of Amyloid with DNP-enhanced MAS NMR Spectroscopy”

Galia Debelouchina, Ph. D.

Princeton University, Princeton, 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: $15 (no charge for students / postdoc / retired / unemployed).

No charge for seminar only.

Extra Door Prizes!

(2 door prizes for # of attendees < 20, 3 door prizes for # of attendees > 20)

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

Abstract:

Amyloid fibrils are insoluble, non-crystalline protein filaments associated with a number of diseases such as Alzheimer’s and Type II diabetes. They can have a functional role in different organisms, and many proteins and peptides have been found to form amyloid fibrils in vitro. This talk will present an overview of what is known regarding their molecular structure, focusing in particular on the fibrils formed by an 11-residue segment from the disease-related protein transthyretin (TTR). This system exemplifies our efforts to characterize the hierarchy of structures present in the fibril form, including the organization of the β-strands into β-sheets (tertiary structure), the β-sheet interface that defines each protofilament (quaternary structure), and the protofilament-to-protofilament contacts that lead to the formation of the complete fibril. Our efforts resulted in the measurement of 110 distance and torsion angle constraints (10 per residue) across all levels of structural organization, resulting in the best resolved amyloid fibril structure so far. The structural investigation benefited extensively from the development of dynamic nuclear polarization, a method used to enhance the sensitivity of MAS NMR experiments, and leading to unprecedented gains in signal-to-noise ratios and acquisition times.

(2 door prizes for # of attendees < 20, 3 door prizes for # of attendees > 20)

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2014-01-22

(Past Events)

Nov 20, 2013 – NMR Topical Group Meeting

The North Jersey ACS NMR Topical Group proudly presents its November monthly meeting at Rutgers CABM on Wednesday, November 20, 2013[ register ]

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 is available in the lot across the street from the CABM building. Dinner will be served in the meeting room.

Featured Speaker

“Protein Dynamics and Biophysical Data Driving Drug Design of Staphylococcus aureus DHFR Inhibitors”

Parag Sahasrabudhe,
CCIE-Structural Biology & Biophysics, Pfizer Global R&D, Groton, CT

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: $15 (no charge for students / postdoc / retired / unemployed).

No charge for seminar only.

Extra Door Prizes!
(2 door prizes for # of attendees < 20, 3 door prizes for # of attendees > 20)

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

Abstract:

DHFR is a classic chemotherapeutic and antibacterial target which has been the subject of numerous structural, protein dynamic and mechanistic studies for over 20 years. A clinically relevant drug resistant mutant, S1 of the Staphylococcus aureus (Sa) ortholog of DHFR has been identified and DHFR inhibitors such as Trimethoprim are about 100-1000 fold less potent against it compared to the wild-type. A loss of enthalpy of interaction between compounds and S1 mutant is detected by isothermal calorimetry. The source of these potency differences are not clearly evident based solely on the low energy static WT and S1 X-ray structures. To address this issue, biophysical methods including NMR solution dynamic studies, in conjunction with thermodynamic, kinetic, computational and structural information are being employed to understand potency differences for both in vitro and whole cell MIC activity studies. Protein dynamics observed by NMR clearly show differences in the binding pockets of WT and S1 proteins as binary and ternary complexes with the cofactor NADPH and Trimethoprim. These differences are not observed in static X-ray structures. Differences observed in us-ms range using relaxation dispersion experiments point to important residues involved in the binding of inhibitor in the substrate binding pocket. Kinetics of binding determined by SPR indicate that the reduction in binding affinities arise from faster off rates and they show correlation to whole cell MICs.

In this presentation, the use of biophysical data to generate hypotheses and to guide chemical design for S1 mutant inhibitors will be highlighted.

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2013-11-20

(Past Events)

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

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