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DNP-NMR Literature Blog

Get up-to-date articles about dynamic nuclear polarization enhanced NMR spectroscopy
(DNP-NMR) and related terahertz technology from scientific journals. A free resource courtesy of Bridge12.

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Dipolar nuclear polarization via the spin diffusion of a dipole order #DNPNMR

Furman, G.B., S.D. Goren, V.M. Meerovich, and V.L. Sokolovsky. “Dipolar Nuclear Polarization via the Spin Diffusion of a Dipole Order.” Journal of Magnetic Resonance 320 (November 2020): 106847.

We propose transfer of the paramagnetic impurity (PI) polarization to nuclei in bulk, outside the diffusion barrier, by using dipolar system of the nuclear spins. The transfer can overcome influence of the diffusion barrier and is proposed to be implemented in four stages. At the first stage, transition of the Zeeman PI order to the Zeeman order of nuclear spins inside the spin-diffusion barrier is occurred. During the second stage the Zeeman order of both the nuclear spins inside the barrier and the nuclear spins in bulk is transferred into the nuclear dipolar spin order. As a result, the nuclear dipolar spin reservoir inside the barrier acquires a lower spin temperature, and thus a gradient of the spin temperature of the nuclear dipolar spin system is created. Since the external magnetic field and the magnetic field created by PIs do not effect on the dipole-dipole interaction between the nuclear spins, the dipolar reservoir is common for all nuclear spins, both inside and outside the diffusion barrier. Restriction of the diffusion barrier is removed and the spin diffusion of the dipole energy and transfer of the spin dipolar order to bulk spins occurs without obstacles (the third stage). At the last stage, to register an NMR signal, the dipolar order of the bulk spins is transferred into the Zeeman order of these spins. Estimations show that enhancement of the polarization can reaches in the case of a 1H nuclear spin, ~220, for 13C ~850, and for 15N ~2130.

Scalable microresonators for room-temperature detection of electron spin resonance from dilute, sub-nanoliter volume solids

This article is about microresonators for EPR Spectroscopy.

Abhyankar, Nandita, Amit Agrawal, Pragya Shrestha, Russell Maier, Robert D. McMichael, Jason Campbell, and Veronika Szalai. “Scalable Microresonators for Room-Temperature Detection of Electron Spin Resonance from Dilute, Sub-Nanoliter Volume Solids.” Science Advances 6, no. 44 (October 2020): eabb0620

We report a microresonator platform that allows room temperature detection of electron spins in volumes on the order of 100 pl, and demonstrate its utility to study low levels of dopants in perovskite oxides. We exploit the toroidal moment in a planar anapole, using a single unit of an anapole metamaterial architecture to produce a microwave resonance exhibiting a spatially confined magnetic field hotspot and simultaneously high quality-factor (Q-factor). To demonstrate the broad implementability of this design and its scalability to higher frequencies, we deploy the microresonators in a commercial electron paramagnetic resonance (EPR) spectrometer operating at 10 GHz and a NIST-built EPR spectrometer operating at 35 GHz. We report continuous-wave (CW) EPR spectra for various samples, including a dilute Mn2+-doped perovskite oxide, CaTiO
3, and a transition metal complex, CuCl2 * 2H2O. The anapole microresonator presented here is expected to enable multifrequency EPR characterization of dopants and defects in perovskite oxide microcrystals and other volume-limited materials of technological importance.

Recent developments in MAS DNP-NMR of materials #DNPNMR

Rankin, Andrew G.M., Julien Trébosc, Frédérique Pourpoint, Jean-Paul Amoureux, and Olivier Lafon. “Recent Developments in MAS DNP-NMR of Materials.” Solid State Nuclear Magnetic Resonance 101 (September 2019): 116–43.

Solid-state NMR spectroscopy is a powerful technique for the characterization of the atomic-level structure and dynamics of materials. Nevertheless, the use of this technique is often limited by its lack of sensitivity, which can prevent the observation of surfaces, defects or insensitive isotopes. Dynamic Nuclear Polarization (DNP) has been shown to improve by one to three orders of magnitude the sensitivity of NMR experiments on materials under Magic-Angle Spinning (MAS), at static magnetic field B0 ≥ 5 T, conditions allowing for the acquisition of high-resolution spectra. The field of DNP-NMR spectroscopy of materials has undergone a rapid development in the last ten years, spurred notably by the availability of commercial DNP-NMR systems. We provide here an in-depth overview of MAS DNP-NMR studies of materials at high B0 field. After a historical perspective of DNP of materials, we describe the DNP transfers under MAS, the transport of polarization by spin diffusion and the various contributions to the overall sensitivity of DNP-NMR experiments. We discuss the design of tailored polarizing agents and the sample preparation in the case of materials. We present the DNP-NMR hardware and the influence of key experimental parameters, such as microwave power, magnetic field, temperature and MAS frequency. We give an overview of the isotopes, which have been detected by this technique, and the NMR methods, which have been combined with DNP. Finally, we show how MAS DNP-NMR has been applied to gain new insights into the structure of organic, hybrid and inorganic materials with applications in fields, such as health, energy, catalysis, optoelectronics etc.

[NMR] Postdoctoral position at NYU (NMR, MRI, magnetometry, spin physics, battery research)

Postdoctoral position at New York University (NMR, MRI, magnetometry, spin physics, battery research) Department of Chemistry

Applications are solicited for an individual to be appointed as an
postdoctoral associate under the supervision of Alexej Jerschow. The research will include one or both of these research areas:

• In-situ and operando NMR/MRI and magnetometry of batteries and
electrochemical devices.
• Study of nuclear spin singlet state life times and singlet relaxation
mechanisms, the development of efficient singlet/triplet conversion pulse sequences and methodology, as well as para-hydrogen induced polarization (PHIP).

Successful applicants must hold a Ph.D. degree in a related field. The ideal candidate will have strong experience in two or more of these areas:

•       NMR or MRI
•       Spin dynamics simulations
•       Machine learning and image processing
•       Hardware/microcontroller/data acquisition set up / programming /operation
•       Magnetometry
•       Electrochemistry
•       Molecular dynamics or ab initio simulations

There is no requirement to master all areas, but depth in two or more areas will enable a good integration with several projects.

Some relevant publications:
•       PCCP 2020, 22, 9703-9712,
•       Chem Mat 2020, 32, 5, 2107-2113
•       PNAS, 2020,
•       JMR 319, 106811, 2020,
•       Sci. Rep. 10, 1-7, 2020,
•       Nat Comm 9:1776, 2018,
•       PNAS, 2016, 113, 10779-84,
•       CPC 2016,
•       JMR 2017, 284, 1-7;
•       PCCP 17, 2015, 24370 – 24375,
•       PCCP, 2019, 21,2595-2600,
•       PNAS, 2019, 116, 18783-18789,
•       JMR 2019, 309, 106601,

There is also an opportunity to be involved in other ongoing projects in the laboratory.

The lab is located in newly renovated facilities of the Molecular Nanoscience Center at NYU’s Washington Square Campus in the heart of Manhattan.

The terms of employment which would be a year, with a possibility of renewal, include a competitive salary and other benefits. Applications will be reviewed on a rolling basis, and candidates will be considered until the position is filled.

To be considered, all applicants must submit a cover letter summarizing research experience and specifying the interests in this position; a curriculum vitae (including a full list of publications); a statement of research interests; and two letters of reference.

Applications should be submitted to:

Alexej Jerschow
Professor of Chemistry
Chemistry Department
New York University
100 Washington Square East
New York, NY 10003
ph: +1 212 998 8451
fax: +1 212 995 4475

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Increased flow rate of hyperpolarized aqueous solution for dynamic nuclear polarization-enhanced magnetic resonance imaging achieved by an open Fabry–Pérot type microwave resonator #DNPNMR

Fedotov, Alexey, Ilya Kurakin, Sebastian Fischer, Thomas Vogl, Thomas F. Prisner, and Vasyl Denysenkov. “Increased Flow Rate of Hyperpolarized Aqueous Solution for Dynamic Nuclear Polarization-Enhanced Magnetic Resonance Imaging Achieved by an Open Fabry–Pérot Type Microwave Resonator.” Magnetic Resonance 1, no. 2 (November 18, 2020): 275–84.

A continuous flow dynamic nuclear polarization (DNP) employing the Overhauser effect at ambient temperatures can be used among other methods to increase sensitivity of magnetic resonance imaging (MRI). The hyperpolarized state of water protons can be achieved by flowing aqueous liquid through a microwave resonator placed directly in the bore of a 1.5 T MRI magnet. Here we describe a new open Fabry–Pérot resonator as DNP polarizer, which exhibits a larger microwave exposure volume for the flowing liquid in comparison with a cylindrical TE013 microwave cavity. The Fabry–Pérot resonator geometry was designed using quasi-optical theory and simulated by CST software. Performance of the new polarizer was tested by MRI DNP experiments on a TEMPOL aqueous solution using a blood-vessel phantom. The Fabry–Pérot resonator revealed a 2-fold larger DNP enhancement with a 4-fold increased flow rate compared to the cylindrical microwave resonator. This increased yield of hyperpolarized liquid allows MRI applications on larger target objects.

Tailored flavoproteins acting as light-driven spin machines pump nuclear hyperpolarization

Ding, Yonghong, Alexey S. Kiryutin, Ziyue Zhao, Qian-Zhao Xu, Kai-Hong Zhao, Patrick Kurle, Saskia Bannister, et al. “Tailored Flavoproteins Acting as Light-Driven Spin Machines Pump Nuclear Hyperpolarization.” Scientific Reports 10, no. 1 (December 2020): 18658.

The solid-state photo-chemically induced dynamic nuclear polarization (photo-CIDNP) effect generates non-Boltzmann nuclear spin magnetization, referred to as hyperpolarization, allowing for high gain of sensitivity in nuclear magnetic resonance (NMR). Well known to occur in photosynthetic reaction centers, the effect was also observed in a light-oxygen-voltage (LOV) domain of the bluelight receptor phototropin, in which the functional cysteine was removed to prevent photo-chemical reactions with the cofactor, a flavin mononucleotide (FMN). Upon illumination, the FMN abstracts an electron from a tryptophan to form a transient spin-correlated radical pair (SCRP) generating the photo-CIDNP effect. Here, we report on designed molecular spin-machines producing nuclear hyperpolarization upon illumination: a LOV domain of aureochrome1a from Phaeodactylum tricornutum, and a LOV domain named 4511 from Methylobacterium radiotolerans (Mr4511) which lacks an otherwise conserved tryptophan in its wild-type form. Insertion of the tryptophan at canonical and novel positions in Mr4511 yields photo-CIDNP effects observed by 15N and 1H liquidstate high-resolution NMR with a characteristic magnetic-field dependence indicating an involvement of anisotropic magnetic interactions and a slow-motion regime in the transient paramagnetic state. The heuristic biomimetic design opens new categories of experiments to analyze and apply the photo-CIDNP effect.

[NMR] Post-doc available in SARS-CoV-2 biochemistry/solid-state NMR – Anja Böckmann, Lyon, France

Postdoctoral Position Available in Protein Solid-State NMR group – Anja Böckmann
MMSB, CNRS-Université Lyon 1, Lyon, France
A postdoctoral position is open at the MMSB in Lyon, France, for a common project with the group of Beat Meier at ETH Zurich, on structural studies of SARS-CoV-2 membrane proteins, including structural and accessory proteins. 
For more info see or
We are looking for an enthusiastic protein biochemist, possibly but not necessarily with a background in NMR, who will work hand in hand with the other post-doc on the project in Zurich. The focus in Lyon will be on the biochemical aspects of the project, including sample preparation and optimization by NMR, as well as studies on interactions/assemblies of the proteins, using cell-free protein synthesis. The work of the post-doc in Zurich will be complemtary, on state-of-the art fast MAS & high field solid-state NMR methods for the analysis of cell-free synthesized protein samples.
A fully equipped wet lab, as well as spectrometers ranging from 500 to 1000 MHz, are available, in particular a 800 WB magnet. 
We seek a candidate who would be ready to start beginning 2021.
For informal queries about the lab and research project, please contact Anja Böckmann by e-mail:
Interested candidates should register their application at

Dr. Anja Böckmann
Protein Solid-State NMR
Molecular Microbiology and Structural Biochemistry
Institut de Biologie et Chimie des Protéines
UMR 5086 CNRS/Université de Lyon
7, passage du Vercors
69367 Lyon Cedex 07

Tel: +33472722649

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Assessment of the Role of 2,2,2-Trifluoroethanol Solvent Dynamics in Inducing Conformational Transitions in Melittin: An Approach with Solvent 19F Low-Field NMR Relaxation and Overhauser Dynamic Nuclear Polarization Studies

Chaubey, Bhawna, Arnab Dey, Abhishek Banerjee, N. Chandrakumar, and Samanwita Pal. “Assessment of the Role of 2,2,2-Trifluoroethanol Solvent Dynamics in Inducing Conformational Transitions in Melittin: An Approach with Solvent 19F Low-Field NMR Relaxation and Overhauser Dynamic Nuclear Polarization Studies.” The Journal of Physical Chemistry B 124, no. 28 (July 16, 2020): 5993–6003.

2, 2, 2-Trifluoroethanol (TFE) is one of the fluoroalcohols that have been known to induce and stabilize open helical structure in many proteins and peptides. The current study has benchmarked low field 19F NMR relaxation and 19F Overhauser Dynamic Nuclear Polarization (DNP) by providing a brief account of TFE solvent dynamics in a model Melittin (MLT; an antimicrobial peptide) solution with TFE: D2O cosolvent mixture at pH 7.4. Further, this approach has been employed to reveal the solvation of MLT by TFE in a nonbuffered solution with a pH 2.8 for the first time. The structural transition of MLT has been elucidated via solvent dynamics by measuring 19F TFE relaxation rates at 0.34 T for various TFE: D2O compositions in absence (bulk TFE) and in presence of MLT at both the pH values. A complementary initial record of Circular Dichroism (CD) experiments on these aqueous MLT solutions with TFE as cosolvent at two different pH conditions demonstrated the structural transition from random coil to helical, or from folded helical to open helical structure. The molecular correlation time derived from corresponding relaxation rates shows that TFE resides on the MLT surface in both pH conditions. However, the trends in the variation of molecular correlation time ratio as a function of TFE concentration represent that the mechanism and the extent to which TFE affects the MLT structural integrity are different at different pH. The extraction of the DNP coupling parameter from steady state 19F ODNP experiments performed in presence of TEMPOL at 0.34 T revealed changes in solvation dynamics of TFE concomitant with MLT structural transition. In summary, 19F relaxation and ODNP measurements made at low field have allowed direct monitoring of TFE dynamics during MLTs structural transition in terms of preferential solvation. The choice of experiments performed at moderately low field (0.34 T) enabled us to exploit on the one hand almost 1200-fold mitigation of the strong contribution of 19F CSA at 11.76 T, while on the other hand the ODNP experiment offered a window for probing molecular dynamics on timescales of the order of 10-1000 picoseconds.

[NMR] 4th webinar of the Early Career Researcher

Dear Colleagues,

The 4th webinar of the Early Career Researcher version of ICMRBS series will take place on Wednesday the 16th December 2020, 12 p.m. PST3 p.m. EDT 8 p.m. GMT 9 p.m. CET /1:30 a.m. IST (India- 17th Dec)/4 a.m. CST (China- 17th Dec) /7 a.m. ADET (Australia- 17th Dec)Please note that the webinar this month has been moved to a different time again to accommodate the speakers from 3 different continents! May I please emphasise again our interest to include ECR speakers from all over the World so wherever you are, if you have an interesting story to tell, please come forward and contact one of our committee.

In this webinar, the three scientific talks on the theme of “Solid State NMR” will be delivered by:
Dr Lauriane Lecoq– CNRS (Lyon, France): The hepatitis B virus capsid seen by solid-state NMR
Dr Marc Sani-The University of Melbourne (Melbourne, Australia): Spin labelled peptide for in-cell DNP solid-state NMR
Asst Prof Andrew Nieuwkoop-Rutgers University (New Jersey, USA): Impacts of protein deuteration and MAS rate on 1H-13C solid-state distance measurements

And for our non-scientific session this month, we are delighted to have Prof Arthur Palmer (Columbia University, USA) who will be sharing his career journey with us. The title of his talk is:Your career from A to Z: Learning from my mistakes

The Zoom link is as below:

Hope to see you all there!


On behalf of the ICMRBS ECR committee
Visit our Website and follow us on Twitter and Instagram!

Contact us to present your work!!!

Angelo Gallo (
Karoline Sanches (
Nick Fowler (
Reid Alderson (
Yanni Chin (

Karoline Sanches Mestre em Biofísica Molecular 
Departamento de Física  Instituto de Biociências, Letras e Ciências Exatas – IBILCE/UNESPSão José do Rio Preto – SP(017)991443193
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[NMR] Ampere Biological Solid-State NMR School

AMPERE Biological Solid-State NMR School

Online Phase: January 13, 2021 – May 26, 2021

Combined Attendance/Online Week:

Berlin, 14.06. -18.06.2021

MDC.C, AXON 1, Robert-Rössle-Str. 10, 13125 Berlin

Dear biological solid-state NMR enthusiast, we will have our biannual Ampere Biological Solid-State NMR School again in 2021! It will be a bipartite course, with an online school of basics from January to May 2021, and a scientific get-together in June 2021. Registration for combined virtual and real event is 40 €, including AMPERE membership. Depending on the situation, the workshop in Berlin will be held under distance-enforcing conditions and participant attendance may be limited to 40 persons. The workshop is geared towards the exchange of experience and nitty-gritty experimental details as well as for networking among PhD students and postdocs. The lectures will be transmitted for those who cannot travel. Students are strongly encouraged to present a poster, but it is of course not required for participation since the course is also designed for newcomers in biological solid-state NMR.

The program features introductory lectures twice a month on Wednesdays from 15:00 to 16:00. There will be a 60 minutes presentation and 15 minutes for the discussion/question session, as well as exercises supplied. Afterwards virtual poster presentations of two participants will take place, 10 mins presentation, 10 mins discussion. In the following week, the exercises on the topic of the lecture will be discussed, again on Wednesdays, 15:00, and solutions presented.

All attendees agree to join the conference dinner on Wednesday, June 16, either in person or via the web. Tables will be arranged outdoors in Berlin and online.


Please send an email to: . This should include the full name, affiliation (full address) and in case you would like to present a poster, send the title. You will receive a request for payment after confirmation of registration. Places are limited.

Program (detailed version under:

13.01              Quantum Mechanics Beat Meier
20.01              Exercises Quantum Mechanics
27.01              Anisotropic Interactions and MAS Beat Meier
03.02              Exercises Anisotropic Interactions
10.02               Time-Dependent Hamiltonians Matthias Ernst
17.02               Exercises Time-Dependent Hamiltonians
24.02               Solving Time-Dependent Hamiltonians Matthias Ernst
03.03              Exercises Solving Time-Dependent Hamiltonians
10.03              Linewidths Basics/Relaxation Beat Meier
17.03              Exercises Linewidths Basics
30./31.03        Product Operator Calculations for Biochemists Hartmut Oschkinat
07.04              SIMPSON Thomas Vosegaard
14.04              Exercises SIMPSON
21.04               Introduction into EPR Enrica Bordignon
28.04              Exercises EPR
05.05               Dynamic Nuclear Polarisation Bob Griffin  
12.05              Exercises Dynamic Nuclear Polarisation
19.05              The Challenges of Modern Structural Biology Huub de Groot
26.05              Installation of CCPN Vicky Higman/Anja Böckmann

Combined Attendance/Online Week:

The lecture slots are 1h30, except for Friday afternoon, some include exercises and sometimes lectures are 2×45 mins, with a separate exercise section.

Recoupling Theory  Ernst
Carbon Detection/Assignments/CCPN Böckmann/MeierThe Spectrometer/Probes  EngelkeDNP   GriffinStructure Calculation Basics  Bardiaux/Higman
10:30-11:00 Coffee Coffee Coffee Coffee Coffee
11:00-12:30Decoupling/Recoupling    VosegaardProton Detection & Fast MAS  Meier/BöckmannSample Prep Bacteria/ Cell-free Böckmann/OschkinatIntegrative Ensemble Calculations Bonomi Structure   Oschkinat/Meier
12:30-14:00 Lunch Lunch Lunch Lunch Lunch
14:00-15:30Exercises   Ernst/VosegaardAssignment Procedures/CCPN  Böckmann//HigmanRelaxation/Dynamics  ReifStudentsPoster Talks(online)Low Populated StatesJensenEPR in Structural BiologyBordignon
15:30-16:00 Coffee Coffee Coffee  In cell MAS NMR Baldus
16:00-17:30Pulse Sequences  PolenovaExercises  Polenova/MeierIntegrative Structural Biology A. LangeStudents Poster Talks(online) 
17:30-18:00 WelcomeMixer(outdoors)QuestionsQuestions (30 mins)Students Poster TalksConference Dinner (outdoors)Questions (online) 

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