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An Upcoming University-funded NMR Facility Manager position at The City University of New York

The City College of New York (CCNY) is accepting applications for a university-funded Senior Research Associate who will serve as an NMR Facility Manager at The City University of New York’s City College (CUNY’s CCNY) in New York City. The successful candidate will have primary responsibility for overseeing the operation of a 3-channel 600 MHz Bruker AVANCE NEO spectrometer equipped for solid-state NMR (1.6-mm and 3.2-mm MAS probes) and a broadband diffusion probe (5-mm, 17 T/m gradients), including applications to both natural biopolymer composites and engineered materials. In addition, the Manager will share secondary responsibility for a 300 MHz Bruker AVANCE III HD walk-up spectrometer with a broadband liquid-state NMR probe and a Quantum Technology helium recycling unit. The Manager will articulate collaboratively with faculty, postdoctoral scientists, Ph.D. research trainees, and undergraduate Honors students to facilitate cutting-edge research and promote interaction among groups that make intensive use of solid-state and biomolecular NMR. The successful candidate will assist in the maintenance and troubleshooting of NMR hardware and software, instrument scheduling, and the implementation and analysis of experiments conducted at CCNY, CUNY’s Advanced Science Research Center, and the adjoining New York Structural Biology Center (NYSBC).

Qualifications for this position include a Ph.D. in Chemistry, Chemical Engineering, Physics, or related disciplines. A minimum of two (2) years of postdoctoral work experience with demonstrated research abilities is preferred. The successful candidate should have experience in one or more of the following areas: solid-state and/or biomolecular NMR applications, NMR instrumentation, and/or NMR facility management. The successful candidate should have a track record of collaborative research on biomacromolecular assemblies and/or materials science.

This position offers abundant access to a host of NMR and other facilities for structural biology, nanoscience, and related research endeavors. Full-featured Bruker NMR spectrometers operating at 600, 700, and 800 MHz are available at the CUNY Advanced Science Research Center (ASRC) adjoining the CCNY NMR Facility in CCNY’s Center for Discovery and Innovation (CDI). Excellent state-of-the-art 500-900 MHz Bruker NMR and 600 MHz DNP facilities, along with rich scientific interactions, are accessible at the world-class NYSBC located on our campus. CCNY hosts CUNY’s Macromolecular Assemblies and Energy Research Institutes as well as faculty-led research groups focusing on biochemistry, biophysics and biodesign (B³), nanoscience, energy, materials, and engineering applications located in CCNY’s Division of Science, Grove School of Engineering, and CUNY Medical School. CUNY’s research community includes several hundred chemists, biologists, physicists, medical researchers, and both chemical and biomedical engineers who interact within a university network of 25 colleges and professional schools. Located in the historic Hamilton Heights – Sugar Hill section of upper Manhattan, CCNY is accessible by major subway and bus lines within the metropolitan New York area.

Information on the initial salary range and benefits package are detailed under Job Opening ID #28663 at https://cuny.jobs. Only applications submitted through the CUNYfirst portal will be considered for this position. Please apply as follows:

- Go to https://cuny.jobs/

- Search for Job Opening ID number: 28663

- Click on the "Apply Now" button and follow the instructions.

Applications must include the following items:

-  Cover Letter

- Curriculum Vitae including refereed publications

- Names and Contact Information for two professional references

CUNY encourages people with disabilities, minorities, veterans and women to apply.  At CUNY, Italian Americans are also included among our protected groups.  Applicants and employees will not be discriminated against on the basis of any legally protected category, including sexual orientation or gender identity. EEO/AA/Vet/Disability Employer.

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Dr. Ruth. E. Stark
Director, CUNY Institute for Macromolecular Assemblies
Distinguished Professor and Member of Doctoral Faculty
Professor,  Department of Chemistry and Biochemistry, The City College of New York (CCNY)

Standard Mail: Marshak Science Building MR-1024
CCNY, 160 Convent Avenue
New York, NY 10031 USA

Packages: CDI Building 1.302
CCNY, ASRC, 85 Saint Nicholas Terrace
New York, NY 10031 USA

Phone: +1-212-650-8916;  +1-212-650-6107
email rstark@ccny.cuny.edu
https://resgroup.ccny.cuny.edu

https://mma.ccny.cuny.edu

https://www.ccny.cuny.edu/grise

https://www.b3-ramp.ccny.cuny.edu

https://www.nanobionyc.com

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Due to a withdrawal, a doctoral funding opportunity in structural biology is still available within the NMR and Modelling Team of the UMR 6014 CNRS COBRA laboratory (U. of Rouen Normandy), in collaboration with Pr. P. Van der Wel's laboratory (U. of Groningen, Netherlands).

Title :
Analysis of turn-rich bioactive peptide properties through an approach combining solution and solid-state NMR and theoretical calculations

Summary :
Bioactive peptides have emerged as a promising class of drugs in the field of pharmacology, due to their specificity and their capacity to selectively target distinct biological processes. Their use as therapeutic agents has become widespread, with various administration routes (dry or wet forms). An important question is how the peptide structure may be affected by the nature of the formulation.
The main objective of this project is to evaluate the impact of the physical state of bioactive peptides, especially those rich in turns in drug preformulation stages.  To this end, we plan to develop an approach combining liquid and solid-state NMR, as well as theoretical calculations. We will first investigate the complementarity of liquid and solid-state NMR in beta-turn characterization using model peptides. Then we will apply the developed methodologies to bioactive peptides of interest.

Host laboratories & research environment
The student will be based at the COBRA laboratory (https://www.lab-cobra.fr/). The lab is localized in the Mont Saint Aignan University campus (https://www.univ-rouen.fr/university-of-rouen-normandy/), in the North west of Rouen (France).
The selected candidate will be recruited and register for the PhD program at the University of Rouen Normandie. He/she will benefit from the state-of-the-art analytical instrumentation park available at the COBRA laboratory for liquid NMR structural biology studies (including liquid/solid state NMR 600 MHz spectrometer, liquid state NMR 600 MHz spectrometer equipped with a cryoprobe, liquid CD spectrometer). He/She will have access to the CRIANN (Centre Régional Informatique et d'Applications Numériques de Normandie) Computing Center for theoretical calculations and will benefit from Dr. V. Tognetti expertise for calculation analyses.
He/She will be welcome at the University of Groningen for few months in Pr. P. Van Der Wel’s laboratory, who has recognized expertise in the study of biomolecules using solid state NMR.

Eligibility
The applicant should have a Master Degree with a speciality in Analytical Chemistry, Physical Chemistry or Structural Biology. He/She must also have taken courses on NMR spectroscopy. Crystallization, peptide/protein NMR or molecular modeling knowledge would be an asset. Fluency in English (both oral and written) is mandatory.

Application procedure and complementary information:
Applications should be sent by e-mail to Isabelle SEGALAS-MILAZZO (isabelle.milazzo@univ-rouen.fr) and Laure GUILHAUDIS (laure.guilhaudis@univ-rouen.fr) and should include: - A detailed CV
- A cover letter
- A short summary of past research accomplishments
- Transcripts of Master grades
- Two recommendation letters or contact details of two referees.

Application deadline: 12/07/2024.

Expected starting date: 01/10/2024

Contacts:
Pr. Isabelle SEGALAS-MILAZZO, Tel: + 33 2 35 52 29 48, e-mail: isabelle.milazzo@univ-rouen.fr
Dr. Laure GUILHAUDIS, Tel:  + 33 2 35 52 29 34, e-mail: laure.guilhaudis@univ-rouen.fr
Dr. Vincent TOGNETTI, e-mail: vincent.tognetti@univ-rouen.fr
Pr. Patrick VAN DER WEL, e-mail: p.c.a.van.der.wel@rug.nl

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Dear All,

We have two open PhD scholarships:

1. Development of Magnetic Resonance Equipment for On-Line Minerals Detection

Link:

https://www.westernsydney.edu.au/schools/grs/scholarships/current_scholarships/current_scholarships/development_of_magnetic_resonance_equipment_for_on-line_minerals_detection_applications

Shortlink:

https://tinyurl.com/43au9j8s

1. Macadamia Genotype Characterisation for Tolerance to Flooding

Link:

https://www.westernsydney.edu.au/schools/grs/scholarships/current_scholarships/current_scholarships/macadamia_genotype_characterisation_for_tolerance_to_flooding

Shortlink:

https://tinyurl.com/3j8uyw5b

Both have closing dates of 31 July 2024 (11.59pm AEST).

I would be grateful if you could circulate this information to potential candidates.

Regards

Bill

_______________________________________________________________
Prof. William S. Price
Professor of Medical Imaging Physics
Nanoscale Organisation and Dynamics Group | School of Science
Building 21.G.45, Campbelltown Campus, Western Sydney University
Locked Bag 1797, Penrith NSW 2751, Australia
P: +61 2 4620 3336 | M: +61 404 830 398 | E: w.price@westernsydney.edu.au
westernsydney.edu.au/nanoscale | anif.org.au

ORCID 0000-0002-8549-4665

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3-year postdoc and 4-year PhD studentship in Multiscale simulation of magnetic hyperpolarisation

The NMR Research Unit at the University of Oulu, Finland, invites applications for a three-year postdoctoral position and a four-year PhD studentship in spin physics and magnetic resonance theory.

Modern nuclear magnetic resonance (NMR) spectroscopy employs different spin hyperpolarisation techniques to enhance the sensitivity by several orders of magnitude as compared to the thermal equilibrium situation. In these positions the successful candidate will develop and apply a multiscale modelling paradigm to investigate the microscopic mechanisms of various hyperpolarisation processes, and contribute to their understanding and development. In the approach one combines molecular dynamics simulations of atomic motion, quantum chemistry calculations to define the spin Hamiltonian from the instantaneous simulation snapshots, and spin dynamics simulations of the density matrix, driven by these Hamiltonians. From the density matrix one calculates observables such as NMR spectra and magnetisation dynamics (e.g., relaxation) from first principles, to compare directly with the primary experimental results, hence realising true computational spectroscopy.

For the postdoctoral position we require a doctoral degree in physics, physical/theoretical/computational chemistry, materials science, or a related field. For the PhD student position a corresponding MSc degree (or equivalent) is required. In both positions the successful candidate has experience in quantum and statistical mechanics, as well as scientific computing. Knowledge of quantum chemistry, spin dynamics, molecular dynamics, or reaction kinetics is considered a merit.

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PhD position starting 2024/2025 in the group of Martin Blackledge at the Insititut de Biologie Structurale (IBS), Grenoble, France

NMR STUDIES OF MOLECULAR DYNAMICS AND DISORDER IN THE VIRAL REPLICATION MACHINERY OF SARS-COV-2

The nucleoprotein (N) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is important for genome replication, encapsidating the viral genome and regulating gene transcription. The central disordered domain is essential to the function of this highly dynamic protein, interacting with the viral protein nsp3,¹ and containing a number of important mutations that are responsible for enhanced viral fitness, and comprising a region that is hyperphosphorylated during the viral cycle. NMR spectroscopy is the tool of choice for studying the conformational behaviour of intrinsically disordered proteins, an abundant class of proteins that are functional in their disordered form. They represent 40% around of all known proteomes and are too dynamic to be studied by crystallography or electron microscopy. The host lab has developed a large number of unique NMR-based tools to help understand the function of this class of proteins at atomic resolution.^2–11  We will use state-of-the-art NMR spectroscopy, small angle scattering and electron microscopy, in combination with molecular simulation, to describe the interactions of N with host and viral partner proteins and viral RNA. The results will be correlated with light and electron microscopy, and fluorescence spectroscopy carried out in collaboration. In addition, the druggability of intrinsically disordered regions of the viral replication machinery is an important, but essentially untapped source of new inhibitory strategies that will be addressed by this project.

1. Bessa, L. M. et al. The intrinsically disordered SARS-CoV-2 nucleoprotein in dynamic complex with its viral partner nsp3a.Science Advances 8, eabm4034 (2022).
2. Bernado, P. et al. A structural model for unfolded proteins from residual dipolar couplings and small-angle x-ray scattering. Proc Natl Acad Sci 102, 17002–17007 (2005).
3. Salmon, L. et al. NMR Characterization of Long-Range Order in Intrinsically Disordered Proteins. J. Am. Chem. Soc. 132, 8407–8418 (2010).
4. Jensen, et al. Exploring free-energy landscapes of intrinsically disordered proteins at atomic resolution using NMR spectroscopy.Chem. Rev. 114, 6632–6660 (2014).
5. Abyzov, A. et al. Identification of Dynamic Modes in an Intrinsically Disordered Protein Using Temperature-Dependent NMR Relaxation. J. Am. Chem. Soc. 138, 6240–6251 (2016).
6. Milles, S. et al. An ultraweak interaction in the intrinsically disordered replication machinery is essential for measles virus function. Science Advances 4, eaat7778 (2018).
7. Adamski, W. et al. A Unified Description of Intrinsically Disordered Protein Dynamics under Physiological Conditions Using NMR Spectroscopy. J. Am. Chem. Soc. 141, 17817–17829 (2019).
8. Guseva, S. et al. Measles virus nucleo- and phosphoproteins form liquid-like phase-separated compartments that promote nucleocapsid assembly. Science Advances 6, eaaz7095 (2020).
9. Camacho-Zarco, et al. Molecular basis of host-adaptation interactions between influenza virus polymerase PB2 subunit and ANP32A. Nature Communications 11, 3656 (2020).
10. Camacho-Zarco, et al. NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins. Chem. Rev. (2022)
11. Guseva, S. et al. Liquid–Liquid Phase Separation Modifies the Dynamic Properties of Intrinsically Disordered Proteins. J. Am. Chem. Soc. 145, 10548–10563 (2023).

The successful candidate will join a multi-disciplinary team investigating the physical role of highly dynamic proteins involved in viral replication, in particular SARS-CoV-2, influenza and measles. The project lies at the interface of biology, chemistry and physics and will combine state-of-the-art NMR spectroscopy with simulation, fluorescence spectroscopy and imaging, X-ray crystallography, cryo-electron microscopy and small angle scattering.

Capital of the French Alps, Grenoble is a world-renowned scientific hub with a strong international flavour. It is a pleasant city, situated at the foot of three mountain ranges offering many possibilities for cultural, outdoor and sporting activities throughout the year. Grenoble is close to the French riviera, Italy and Switzerland and is served by international airports and a high-speed rail network

Interested candidates (biochemists, chemists or biophysicists) should send a cv and motivation letter to martin.blackledge@ibs.fr

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Dear all,

https://jobs.le.ac.uk/vacancies/9767/research-associate.html

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