Category Archives: ssNMR

[NMR] Radboud University Nijmegen is searching for a tenure-track assistant professor Physical Chemistry, Solid State NMR Spectroscopy

Tenure-track Assistant Professor of Physical Chemistry, Specialising in Solid-state NMR Spectroscopy

  • 32 – 40 hours per week
  • Maximum gross monthly salary: € 5,127
  • Faculty of Science
  • Required background: PhD
  • Duration of the contract: 6 years
  • Application deadline: 27 September 2020

We are looking for
As a researcher, you will build up a research group that is able to attract research funding and provide supervision and guidance to undergraduate and graduate students and PhD candidates. Your teaching activities – with a focus on teaching physical chemistry and NMR methods – will be part of the Education Institute for Molecular Sciences, which is responsible for the Bachelor’s and Master’s degree programmes in Chemistry, Molecular Life Sciences and Science.

Your research must fit in with the research activities of the Institute for Molecules and Materials (IMM). A unique aspect of the current research programme is that methods development is combined with realistic applications in materials science such as energy materials (Li-battery materials, hydrogen storage materials), catalysis, and polymers. We wish to expand this research to applications in soft matter, linking up with research in IMM on soft nanotechnology, self-assembly, and/or understanding the underlying principles of soft matter in a biomimetic context. A key aspect for unravelling structure-function relations in soft matter is the ability to probe local molecular interactions and dynamics. Characterisation at the molecular scale and the development of constitutive models are needed to aid new developments in this field. Novel NMR methodology and particularly the recent surge of methodological developments in solid-state 1H NMR and hyperpolarised magnetic resonance offer novel opportunities.

We ask
An enthusiastic scientist with research skills in the field of solid-state NMR spectroscopy, who wants to build up their own research group within IMM.
A lecturer who will participate in our faculty’s educational programmes.
A background in solid-state NMR demonstrated by publications and presentations at international conferences.

We are
The Institute for Molecules and Materials (IMM) is a research institute in chemistry and physics, which fosters interdisciplinary research. Its mission is to design and create functional molecules and materials to fundamentally understand their behaviour. IMM comprises 19 research groups active in areas ranging from condensed matter science to organic chemistry and chemical biology. We focus on fundamental research with an open eye for societal applications and educate the next generation of leaders in science and innovation.
IMM distinguishes itself from similar institutes by intense collaborations and interactions between chemists and physicists and between experimentalists and theorists. IMM has a strong infrastructure including large user facilities such as the High Field Magnet Laboratory (HFML), the Free Electron Laser facility FELIX and part of the uNMR-NL facilities.

You will be part of the Magnetic Resonance Research Centre, headed by Prof. Arno Kentgens, where research is focused on fundamentally new solid- and liquid-state NMR methodology and its application to functional materials and the analysis of complex mixtures. The centre hosts the national solid-state NMR facility for advanced materials science that is embedded in the national uNMR-NL facility. It has a range of state-of-the-art spectrometers at its disposal, including 300, 400, 600 and 850 MHz solid-state and 400, 500 and 600 MHz liquid-state NMR spectrometers. Dynamic nuclear polarisation capabilities are available at 400 MHz/263 GHz and 600 MHz/396 GHz. These spectrometers are equipped with a host of commercial and home-built probes, making it possible to detect numerous nuclei and materials. The centre has unique expertise on the development of miniaturised NMR probe technology. As of 2021, MRRC will house the uNMR-NL 950 MHz spectrometer, which has solid-state, liquid-state and micro-imaging capabilities. Furthermore the uNMR-NL consortium is among the first to get a 1.2 GHz spectrometer.

Radboud University

We want to get the best out of science, others and ourselves. Why? Because this is what the world around us desperately needs. Leading research and education make an indispensable contribution to a healthy, free world with equal opportunities for all. This is what unites the more than 22,000 students and 5,000 employees at Radboud University. And this requires even more talent, collaboration and lifelong learning. You have a part to play!
We offer
Employment: 32 – 40 hours per week.
A gross monthly salary from a minimum of €3,746 to a maximum of €5,826 based on a 38-hour working week (scale 11-12). The exact salary depends on your qualifications and amount of relevant professional experience.
In addition to the salary: an 8% holiday allowance and an 8.3% end-of-year bonus.
Further information on a tenure track at the Faculty of Science can be found here.
Duration of the contract: you will be appointed for a six-year period; after positive evaluation, you may be offered a permanent contract.
The intended start date is 1 January 2021.
You will be able to make use of our Dual Career Service: our Dual Career Officer will assist with family-related support, such as child care, and help your partner prepare for the local labour market and with finding an occupation.
Are you interested in our excellent employment conditions?
Would you like more information?

For more information about this vacancy, please contact:
Prof. Jana Roithová, Professor Spectroscopy and Catalysis
Email: roithova-office@science.ru.nl

prof. A. Kentgens,
Tel.: +31 24 365 52078
Email: a.kentgens@nmr.ru.nl
Apply directly

Please address your application to Prof. Jana Roithova and submit it, using the application button, no later than 27 September 2020, 23:59 Amsterdam Time Zone.

Your application should include the following attachments:

A motivation letter.
Your CV including a list of publications and the names and contact details (including email addresses) of three potential references.
A selection of 3-5 of your most significant publications, along with brief descriptions thereof (please do not attach the original manuscripts).
A research statement, including a description of how your research programme will add novel aspects to, and align with, IMM’s research programme (maximum 2 pages).
A teaching statement (maximum 1.5 pages).

The first round of interviews will take place between 12 October and 18 October 2020.

For application, please see: https://www.ru.nl/werken-bij/vacature/details-vacature/?recid=1122917&doel=embed&taal=nl

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ICMRBS: Emerging MR Webinar, June 18

Dear Colleagues:

In lieu of an in-person meeting this summer, ICMRBS is supporting a weekly webinar series in biological magnetic resonance (http://emergingmr.org) with weekly talks on Thursday afternoons (Europe) / mornings (N. America). For Thursday, June 18:

Tuo Wang (Louisiana State University)
Elucidation of carbohydrate structure in plant biomass and fungal pathogens using solid-state NMR and DNP methods

Rina Rosenzweig (Weizmann Institute of Science)
Molecular Chaperones in Protein Disaggregation – What we can learn from NMR

June 18: 7 a.m. PST / 10 a.m. EST / 4 p.m. CEST / 7.30 p.m IST / 10 p.m. CST
https://zoom.us/j/91219438807?pwd=NHZnbUZHZ1d0YW1YcStJU2t0dlBEdz09
Webinar-ID: 912 1943 8807 Password: bioNMR2020

Prior talks are posted to the ICMRBS’ YouTube channel ca. 1 week post presentation (https://www.youtube.com/channel/UCsxup-QiNEeBrfo-4d5w33Q).

Please spread the word and share this email with your colleagues! If you’ve received this email indirectly, please email kgardner@gc.cuny.edu to be added to the mailing list.

Best regards,
Kevin Gardner on behalf of ICMRBS Council

[NMR] 5th DNP/NMR Educational Tutorial, June 05/ Dr. Yusuke Nishiyama from JEOL

Dear NMR Enthusiast,

We are happy to announce the 5th Educational Tutorial. 

This week Dr. Yusuke Nishiyama, JEOL, Japan will talk about 

“Practical aspects of Fast MAS Solid-State NMR”.

Here are the webinar details:

Time: Friday, June 05, 2020, 07:00 AM California or 10:00 AM Boston or 4:00 PM Paris or 11:00 PM Tokyo

Join Meeting: https://ucsb.zoom.us/j/95617252728

Meeting ID: 956 1725 2728

The current format of the tutorial will consist of a 35-minute talk which will include both basic and advanced material and 25 minutes of discussion. Prof. Vipin Agarwal, TIFR Hyderabad, India will be a special panelist in the discussion session.

Please note that we have advanced the timing of (only) this session by 90 minutes for Speaker’s convenience.

Best regards,

Global NMR Discussion Meetings

PS. 

We are glad that you are liking our tutorials. In case you want to hear it again, here is the link to our previous sessions:

https://www.youtube.com/channel/UCMDyuVI6NMYzR3LByZWP4sg

Please subscribe to our YouTube channel.

[Organizers:

Adrian Draney (Guido Pintacuda Lab, CRMN lyon)

Amrit Venkatesh (Aaron Rossini Lab, Iowa)

Asif Equbal (Songi Han Lab, UCSB)

Blake Wilson (Robert Tycko Lab, NIH)

Daphna Shimon (Ilia Kaminker Lab, Tel Aviv)

Michael Hope (Lyndon Emsley Lab, EPFL)

Mona Mohammadi (Alexej Jerschow, NYU)

PinelopiMoutzouri (Lyndon Emsley Lab, EPFL) ]

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ssNMR/DNP ZOOMinar: Aaron Rossini (Iowa) and Evan Wenbo Zhao

Hi all,

Bob and I would like to announce our upcoming ZOOMinar session on 3rd June, Wed. Our speakers are Prof. Aaron Rossini (Iowa State University) and Evan Wenbo Zhao (Clare Grey?s group, Univ. of Cambridge), the details are:

Zoom link: https://mit.zoom.us/j/95833202637 <https://mit.zoom.us/j/95833202637>

Date/ Time: Wed 3rd June, 8.00 am California/ 11.00 am Boston/ 5.00 pm Paris/ 6.00 pm Israel

Further details about the ZOOMInar available at <https://griffingroup.mit.edu/weekly-ssnmrdnp-zoominar>https://griffingroup.mit.edu/weekly-ssnmrdnp-zoominar <https://griffingroup.mit.edu/weekly-ssnmrdnp-zoominar>

1st speaker: Evan Wenbo Zhao, ?In Situ NMR and EPR Studies of Anthraquinone-Based Redox Flow Batteries?

(*Attachment available at

https://www.dropbox.com/sh/h89pj8hd1ky4o1g/AADO6YyprC_uNd4H7aHxFpppa?dl=0 <https://www.dropbox.com/sh/h89pj8hd1ky4o1g/AADO6YyprC_uNd4H7aHxFpppa?dl=0>*)

Postdoc with Clare P. Grey at Univ. of Cambridge

PhD with Clifford Russell Bowers at Univ. Florida

Undergraduate at Nanyang Technological University

2nd speaker: Prof. Aaron Rossini, ?Characterization of Nanomaterials by Sensitivity-Enhanced Solid-State NMR Spectroscopy?

Assistant Professor at Iowa State University

Postdoc with Lyndon Emsley and Anne Lessage at ENS Lyon / EPFL

Undergraduate/PhD with Rob Shurko at Univ. of Windsor

Regards,

Kong and Bob

Dr. Kong Ooi Tan

Postdoctoral Fellow

Francis Bitter Magnet Laboratory

Massachusetts Institute of Technology

77 Massachusetts Avenue, NW14-4112

Cambridge, MA 02139

[ssNMR] Post-doc position in the Nieuwkoop Lab

The Nieuwkoop lab seeks a post-doctoral researcher to help start a project on the structural biology of the PTEN protein. We use fast spinning solid-state NMR to study protein-lipid interactions. In this project, we seek to understand the functional role of PIP binding by the C2 domain of PTEN. The PTEN C2 domain will be expressed with isotopic labeling to for backbone and side-chain NMR assignments as nanocrystals and bound to its PIP ligand in liposomes. This project will depend on novel ssNMR experiments, optimized sample preparation, and specialized NMR equipment to assess structural and dynamical changes in the bound and unbound protein.

Contact Andy at an567@chem.rutgers.edu for more details and apply here: http://jobs.rutgers.edu/postings/101163

[NMR] Postdoc in biomolecular solid-state NMR in Strasbourg, France

Postdoctoral Position: Biomolecular Solid-state NMR 

The laboratory Membrane Biophysics and NMR at the University of Strasbourg has an opening for a postdoctoral position with experience in using solid-state NMR for the analysis of peptides and proteins. The aim of the project is to reveal the structural determinants that define the highly specific lipid recognition motif of a transmembrane protein and to characterize changes in structure, dynamics, oligomerization and topology of the protein as well as the lipids during recognition. Another ongoing project is the structural investigation of peptide fibers with strong nucleic acid and lentiviral transfection potential.

Candidates should have good experience in biomolecular solid-state NMR. Other techniques of the laboratory are solution NMR approaches, various types of biophysical methods, peptide synthesis and/or the biochemical production of proteins. Knowledge in some of these latter techniques are of advantage. S/he should have an interest in working in a highly interdisciplinary, international and collaborative environment. The project and position are funded by a three-year grant from the French National Agency for Research (ANR). The University of Strasbourg chemistry, life sciences and structural biology departments have excellent scientific records, with a multitude of collaborations world-wide.

Strasbourg is a very nice city on the French side of the Rhine river, at the border to Germany, with easy access to nearby mountains (Vosges, Black Forrest, Alps). Being in the heart of Europe it takes only short train rides to multiple destinations of scientific and/or touristic interest. 

Candidates should send their CV, publication list and contact info for three references to:

Prof. Burkhard Bechinger,

bechinger@unistra.frWeb Sites: www-chimie.u-strasbg.fr/~rmnmc

www.icfrc.fr/en/

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[NMR] Postdoctoral position in Lewandowski group at University of Warwick, UK – solid-state & solution NMR of natural products megasynthesases

A 2-year ERC-funded postdoc position is available in the Lewandowski group (http://go.warwick.ac.uk/lewandowskigroup) in the Department of Chemistry at the University of Warwick, United Kingdom.

Duration: 2 years | Start: Aug-Sept 2018 | Application deadline: 22 June 2018

Link to the full advertisement and application: https://atsv7.wcn.co.uk/search_engine/jobs.cgi?owner=5062452&ownertype=fair&jcode=1727027&vt_template=1457&adminview=1

The applicant will work on a major ERC-funded project employing combination of chemical biology, solid-state and solution-state NMR to study the structures, dynamics and interactions of domains from within polyketide synthases in order to facilitate their rational engineering for synthetic biology applications. Polyketide synthases are multicomponent enzymatic assembly lines for a range of useful natural products, for example, antibiotics that are effective against certain multidrug resistant infections. 

Experience in applying solution and/or solid-state NMR spectroscopy to elucidating the structures and/or dynamics of proteins is advantageous and a good knowledge of techniques for the overproduction and purification of recombinant proteins is essential.

The applicant will join a highly interdisciplinary collaborative team (exposure to a wide range of expertise and high potential for picking up new skills) under the supervision of Józef Lewandowski (http://go.warwick.ac.uk/lewandowskigroup) and in collaboration with Greg Challis (https://warwick.ac.uk/fac/sci/chemistry/research/challis/challisgroup).

Facilities:

The Warwick Laboratory for Magnetic Resonance (http://www2.warwick.ac.uk/fac/sci/physics/research/condensedmatt/nmr/) is a world-class biological and material science magnetic resonance set up hosting 7 academic staff from Physics and Chemistry and housing a suite of 9 solid-state NMR spectrometers (from 100 to 850 MHz; the main spectrometers for the biomolecular applications are 500, 600 and 700 MHz + access to 850 MHz and soon 1 GHz through a national facility at Warwick; a ¾ of 700 MHz solid-state NMR spectrometer time is dedicated to the project), 2 dynamic nuclear polarization (DNP) spectrometers (94 and 200/400 GHz) and advanced EPR instrumentation. A wide range of magic angle spinning probes is available in the laboratory including several 1.3 mm Bruker probes (< 67 kHz spinning), 1 mm JEOL probe, 0.81 mm Samoson probe (100 kHz spinning) and 3x 0.7 mm Bruker probes (111 kHz spinning). Solution NMR facilities include 500, 600 and 700 MHz equipped with cryoprobe (https://warwick.ac.uk/fac/sci/chemistry/research/facilities/nmr/). We have access to the state of the art mass spec facilities (https://warwick.ac.uk/fac/sci/chemistry/research/facilities/massspec) and X-ray crystallography.

The Chemical Biology Research Facility at University of Warwick (https://warwick.ac.uk/fac/sci/chemistry/research/facilities/chembiolfacility/) provides cutting edge infrastructure for organic synthesis, molecular biology, protein chemistry, microbiology, radiochemistry, biophysical and biochemical analysis.

Informal inquiries should be directed to Józef Lewandowski (j.r.lewandowski@warwick.ac.uk) and formal applications submitted (deadline Jun 22 2018). at https://atsv7.wcn.co.uk/search_engine/jobs.cgi?owner=5062452&ownertype=fair&jcode=1727027&vt_template=1457&adminview=1

Another postdoctoral position on a related BBSRC-funded project will become available in June-July 2018.

==========================================================================

Józef R. Lewandowski

Associate Professor | Department of Chemistry | University of Warwick

j.r.lewandowski@warwick.ac.uk | External: +44 (0) 24 76151355 | Internal: 51355 

Chemistry: C519 | Millburn House: F07 | Coventry CV4 7AL | Find us on the interactive map

Lewandowski group website | Warwick solid-state NMR group website

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Direct Evidence of Imino Acid–Aromatic Interactions in Native Collagen Protein by DNP-Enhanced Solid-State NMR Spectroscopy

Singh, C., et al., Direct Evidence of Imino Acid–Aromatic Interactions in Native Collagen Protein by DNP-Enhanced Solid-State NMR Spectroscopy. The Journal of Physical Chemistry Letters, 2014. 5(22): p. 4044-4048.

http://dx.doi.org/10.1021/jz502081j

Aromatic amino acids (AAAs) have rare presence (?1.4% abundance of Phe) inside of collagen protein, which is the most abundant animal protein playing a functional role in skin, bone, and connective tissues. The role of AAAs is very crucial and has been debated. We present here experimental results depicting interaction of AAAs with imino acids in a native collagen protein sample. The interaction is probed by solid-state NMR (ssNMR) spectroscopy experiments such as 1H?13C heteronuclear correlation (HETCOR) performed on a native collagen sample. The natural abundance 13C spectrum was obtained by dynamic nuclear polarization (DNP) sensitivity enhancement coupled with ssNMR, providing 30-fold signal enhancement. Our results also open up new avenues of probing collagen structure/dynamics closest to the native state by ssNMR experiments coupled with DNP.

Matrix-free dynamic nuclear polarization enables solid-state NMR (13)C-(13)C correlation spectroscopy of proteins at natural isotopic abundance

Takahashi, H., S. Hediger, and G. De Paepe, Matrix-free dynamic nuclear polarization enables solid-state NMR (13)C-(13)C correlation spectroscopy of proteins at natural isotopic abundance. Chem Commun (Camb), 2013. 49(82): p. 9479-81.

http://www.ncbi.nlm.nih.gov/pubmed/24013616

We introduce a general approach for dynamic nuclear polarization (DNP) enhanced solid-state NMR that overcomes the current problems in DNP experiments caused by the use of frozen solutions. Notably, we report for the first time a 2D (13)C-(13)C correlation spectrum of a protein without the use of isotopic labeling.

Matrix-free dynamic nuclear polarization enables solid-state NMR (13)C-(13)C correlation spectroscopy of proteins at natural isotopic abundance

Takahashi, H., S. Hediger, and G. De Paepe, Matrix-free dynamic nuclear polarization enables solid-state NMR (13)C-(13)C correlation spectroscopy of proteins at natural isotopic abundance. Chem Commun (Camb), 2013. 49(82): p. 9479-81.

http://www.ncbi.nlm.nih.gov/pubmed/24013616

We introduce a general approach for dynamic nuclear polarization (DNP) enhanced solid-state NMR that overcomes the current problems in DNP experiments caused by the use of frozen solutions. Notably, we report for the first time a 2D (13)C-(13)C correlation spectrum of a protein without the use of isotopic labeling.

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