Jan 18, 2020

[NMR] Training Courses on Paramagnetic NMR and Metal Trafficking

Dear Colleagues,

Please forward this announcement to all your colleagues and to any potential candidate, thank you.

TRAINING COURSE : FUNDAMENTALS OF MAGNETIC RESONANCE SPECTROSCOPIES AND
METAL TRAFFICKING
HANDS-ON WORKSHOP: NMR OF PARAMAGNETIC PROTEINS AND APPLICATIONS

Two Training Events, dedicated to PhD Students and PostDoc working in the field of Biomolecular NMR and/or in Metalloprotein Chemistry, will be organized in the period June 22nd-June 26th at the Magnetic Resonance Center of the University of Florence.

A three days Training Course on Fundamentals of Magnetic Resonance Spectoscopies and Metal Trafficking will be followed by a two Hands-on Workshop on NMR of Paramagnetic Proteins and Applications. Both initiatives are supported by the TIMB3 Project, a Twinning project funded by the European Union. Deadline for application is February 29th.

Please follow the link for the detailed program:

For further information write to: nmrtraining2020@cerm.unifi.it

====================================
This is the AMPERE MAGNETIC RESONANCE mailing list:

NMR web database:

Jan 17, 2020

Targetable Tetrazine‐Based Dynamic Nuclear Polarization Agents for Biological Systems #DNPNMR

Lim, Byung Joon, Bryce E. Ackermann, and Galia T Debelouchina. “Targetable Tetrazine‐Based Dynamic Nuclear Polarization Agents for Biological Systems.” ChemBioChem, November 19, 2019, cbic.201900609.


Dynamic nuclear polarization (DNP) has shown great promise as a tool to enhance the nuclear magnetic resonance (NMR) signals of proteins in the cellular environment. As the sensitivity increases, the ability to select and efficiently polarize a specific macromolecule over the cellular background has become desirable. Here, we address this need and present a tetrazine-based DNP polarization agent that can be targeted selectively to proteins containing the unnatural amino acid (UAA) norbornene-lysine. The UAA can be introduced efficiently by genetic means in the cellular milieu. Our approach is bio-orthogonal and easily adaptable to any protein of interest. We illustrate the scope of our methodology and investigate the DNP polarization transfer mechanisms in several biological systems. Our results shed light on the complex polarization transfer pathways in targeted DNP and ultimately pave the way to selective DNPenhanced NMR spectroscopy in both bacterial and mammalian cells.

Jan 15, 2020

[NMR] ERC-funded PhD positions in small-molecule NMR - Nantes, France #DNPNMR

Dear colleagues,

Three ERC-funded PhD positions are open in the Nantes NMR group of the CEISAM research institute, in the field of small-molecule NMR of complex mixtures.

The PhD students will join a dynamic NMR group and work on two ERC-funded projects led by Jean-Nicolas Dumez and Patrick Giraudeau. The three PhD projects will consist of:

1) developing methods for fast diffusion-ordered NMR spectroscopy (DOSY), based on the principles of spatial encoding (SPEN), for the monitoring of out-of-equilibrium systems. These methods will be applied to reaction monitoring on a variety of chemical systems.

2) developing ultrafast 2D NMR heteronuclear methods for the analysis of complex biological samples hyperpolarized by dissolution dynamic nuclear polarization. The methods will be applied to various research questions in the field of metabolomics.

3) developing a variety of homo- and hetero-nuclear NMR methods for the analysis of out-of-equilibrium complex mixtures involving flow analysis and/or hyperpolarization.

Applicants should have a background in chemistry (preferentially analytical or physical) or physics, and a strong interest in both fundamental and applied aspects of magnetic resonance.
The NMR group of the CEISAM lab works on method developments in solution-state NMR and their application to the analysis of mixtures. It is equipped with state-of-the-art NMR spectrometers, in the 400 to 700 MHz range, a microimaging system and a prototype polariser for dissolution-DNP. CEISAM is the molecular chemistry lab of the Université de Nantes, where research includes physical and analytical chemistry, organic synthesis and catalysis, and chemical biology. The lab is located in the vibrant city of Nantes, close to the Atlantic Coast of south Brittany.

Positions are for three years and will start on October 1st 2020. Please send applications including cover letter, CV and the name of two referees to Jean-Nicolas Dumez and Patrick Giraudeau. The first round of applications will be closed on March 31st.

Please forward this message to potential candidates.


Best regards

Jean-Nicolas Dumez and Patrick Giraudeau

--
Prof. Patrick GIRAUDEAU
CEISAM/Chemistry Department
Faculty of Science and Technology

Tel : (33)251125709

2 rue de la Houssinière BP 92208
44322 Nantes Cedex 3
FRANCE

Be eco-friendly: print this e-mail only if necessary

====================================
This is the AMPERE MAGNETIC RESONANCE mailing list:

NMR web database:

Postdoctoral Position: EPR Spectroscopic Studies of Membrane Proteins #EPR

Postdoctoral Position: EPR Spectroscopic Studies of Membrane Proteins

Miami University, Oxford, OH, USA

A Postdoctoral research position is available immediately to study the structural and dynamic properties of integral membrane proteins in the laboratory of Prof. Gary A. Lorigan in the Department of Chemistry and Biochemistry at Miami University in Ohio. The postdoctoral position is funded through a NIH MIRA R35 grant.

Candidates who are interested in studying the structural and dynamic properties of membrane proteins are encouraged to apply. Experience in two of the following areas is desirable: molecular biology and biochemistry of membrane proteins, protein purification, and EPR spectroscopy. 2 pulsed EPR spectrometers (X-band/Q-band) for DEER and ESEEM experiments, 2 CW-EPR spectrometers, and a 500 MHz solid-state NMR instrument are available for this project. Miami University is home to the Ohio Advanced EPR Lab (http://epr.miamioh.edu). Please send a CV and two letters of recommendation to: Professor Gary A. Lorigan, Department of Chemistry and Biochemistry, Miami University gary.lorigan@miamioh.edu. A Ph.D. in Chemistry/Biochemistry or related fields is required. Contact phone is 513-529-3338. 

Miami University, an Equal Opportunity/Affirmative Action employer, encourages applications from minorities, women, protected veterans and individuals with disabilities. Miami University prohibits harassment, discrimination and retaliation on the basis of sex/gender (including sexual harassment, sexual violence, sexual misconduct, domestic violence, dating violence, or stalking), race, color, religion, national origin (ancestry), disability, age (40 years or older), sexual orientation, gender identity, pregnancy, status as a parent or foster parent, military status, or veteran status in its recruitment, selection, and employment practices. Requests for all reasonable accommodations for disabilities related to employment should be directed to ADAFacultyStaff@miamioh.edu or 513-529-3560.

As part of the University’s commitment to maintaining a healthy and safe living, learning, and working environment, we encourage you to read Miami University’s Annual Security & Fire Safety Report at http://www.MiamiOH.edu/campus-safety/annual-report/index.html(http://www.miamioh.edu/campus-safety/annual-report/index.html), which contains information about campus safety, crime statistics, and our drug and alcohol abuse and prevention program designed to prevent the unlawful possession, use, and distribution of drugs and alcohol on campus and at university events and activities. This report also contains information on programs and policies designed to prevent and address sexual violence, domestic violence, dating violence, and stalking. Each year, email notification of this website is made to all faculty, staff, and enrolled students. Written notification is also provided to prospective students and employees. Hard copies of the Annual Security & Fire Safety Report may be obtained from the Miami University Police Department at (513) 529-2225.


Gary A. Lorigan
John W. Steube Professor 
Department of Chemistry and Biochemistry
Miami University
651 E. High St.
Oxford, Ohio 45056


Office: 137 Hughes Laboratories
Phone: (513) 529-3338
Fax: (513) 529-5715
EPR facility: epr.muohio.edu

====================================
This is the AMPERE MAGNETIC RESONANCE mailing list:

NMR web database:

Disclosing Interfaces of ZnO Nanocrystals Using Dynamic Nuclear Polarization: Sol-Gel versus Organometallic Approach #DNPNMR

Lee, Daniel, Małgorzata Wolska-Pietkiewicz, Saumya Badoni, Agnieszka Grala, Janusz Lewiński, and Gaël De Paëpe. “Disclosing Interfaces of ZnO Nanocrystals Using Dynamic Nuclear Polarization: Sol-Gel versus Organometallic Approach.” Angewandte Chemie International Edition 58, no. 48 (November 25, 2019): 17163–68.


The unambiguous characterization of the coordination chemistry of nanocrystal surfaces produced by wetchemical synthesis presently remains highly challenging. Here, zinc oxide nanocrystals (ZnO NCs) coated by monoanionic diphenyl phosphate (DPP) ligands were derived by a sol-gel process and a one-pot self-supporting organometallic (OSSOM) procedure. Atomic-scale characterization through dynamic nuclear polarization (DNP-)enhanced solid-state NMR (ssNMR) spectroscopy has notably enabled resolving their vastly different surface-ligand interfaces. For the OSSOM-derived NCs, DPP moieties form stable and strongly-anchored m2- and m3-bridging-ligand pairs that are resistant to competitive ligand exchange. The sol-gel-derived NCs contain a wide variety of coordination modes of DPP ligands and a ligand exchange process takes place between DPP and glycerol molecules. This highlights the power of DNP-enhanced ssNMR for detailed NC surface analysis and of the OSSOM approach for the preparation of ZnO NCs.

Jan 13, 2020

Recent Advances in Magic Angle Spinning‐Dynamic Nuclear Polarization Methodology #DNPNMR

Kaminker, Ilia. “Recent Advances in Magic Angle Spinning‐Dynamic Nuclear Polarization Methodology.” Israel Journal of Chemistry 59, no. 11–12 (November 2019): 990–1000.


Dynamic nuclear polarization (DNP) is a method to boost the nuclear magnetic resonance (NMR) signal and thus alleviate the main limitation of NMR spectroscopy-its low sensitivity. One particularly successful methodology is the combination of DNP with magic angle spinning (MAS). MAS-DNP enables orders of magnitude signal enhancements in solid-state NMR experiments. The success of modern MAS-DNP stems from a combination of multiple developments in hardware, polarization agents design, sample preparation, theoretical understanding, and experimental methodology. Altogether these developments have allowed numerous breakthrough applications in biology and materials science. Despite its proven successes, ongoing research aims to further optimize hardware and polarization agent chemistry. Recent advances in MAS-DNP methodology that will allow unprecedented sensitivity in novel future applications are reviewed in this manuscript.

Jan 10, 2020

Hyperpolarization of Amino Acids in Water Utilizing Parahydrogen on a Rhodium Nanocatalyst

Kaltschnee, Lukas, Anil P. Jagtap, Jeffrey McCormick, Shawn Wagner, Louis‐S. Bouchard, Marcel Utz, Christian Griesinger, and Stefan Glöggler. “Hyperpolarization of Amino Acids in Water Utilizing Parahydrogen on a Rhodium Nanocatalyst.” Chemistry – A European Journal 25, no. 47 (August 22, 2019): 11031–35.


NMR offers many possibilities in chemical analysis, structural investigations, and medical diagnostics. Although it is broadly used, one of NMR spectroscopies main drawbacks is low sensitivity. Hyperpolarization techniques enhance NMR signals by more than four orders of magnitude allowing the design of new contrast agents. Parahydrogen induced polarization that utilizes the parahydrogen’s singlet state to create enhanced signals is of particular interest since it allows to produce molecular imaging agents within seconds. Herein, we present a strategy for signal enhancement of the carbonyl 13C in amino acids by using parahydrogen, as demonstrated for glycine and alanine. Importantly, the hyperpolarization step is carried out in water and chemically unmodified canonical amino acids are obtained. Our approach thus offers a high degree of biocompatibility, which is crucial for further application. The rapid sample hyperpolarization (within seconds) may enable the continuous production of biologically useful probes, such as metabolic contrast agents or probes for structural biology.