PhD positions open in biomolecular solid- and solution-state NMR at IST Austria

Three PhD positions in Biomolecular NMR are open in the Schanda group at the Institute of Science and Technology Austria (ISTA)

Use solution- and solid-state NMR to address chaperone function and protein translocation

We study how chaperones assist other proteins to fold, and how a network of chaperones, co-chaperones and receptor domains assists protein import into mitochondria. You will decipher e.g. the functional mechanisms by which the very dynamic protein-import machinery is able to efficiently insert proteins into mitochondria - or to clear up proteins in cases where the machinery gets clogged. The complexes we study comprise soluble chaperones, membrane-embedded insertases, as well as the to-be-imported proteins; we have developed approaches to generate such complexes efficiently. You will combine solution- and magic-angle spinning (MAS) NMR with biochemistry and biophysics, as well as cellular experiments, together with our international collaborators.

Relevant publications from our group:

Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space. Cell 175(5): 1365-1379 https://www.cell.com/cell/fulltext/S0092-8674(18)31395-3; highlighted in  https://f1000.com/prime/734441988

Architecture and assembly dynamics of the essential mitochondrial chaperone complex TIM9·10·12. Structure2021, 29: 1-9. https://doi.org/10.1016/j.str.2021.04.009

Structural basis of client specificity in mitochondrial membrane-protein chaperones., Science Advances. 2020, 6, 51: eabd0263 , https://advances.sciencemag.org/content/6/51/eabd0263

Develop and apply MAS NMR to study how dynamics underlies protein function, and how evolution shaped allostery

Protein dynamics are essential for their function. We use MAS NMR to probe the dynamics or large enzymatic complexes, often hundreds of kilodaltons in size. By determining motions at residue-specific resolution, we probe, for example, the presence of transient, low-populated states and their relevance for function. In the ongoing projects we address how evolution has shaped protein dynamics and how processes such as allosteric regulation are rooted in dynamic coupling of different parts of an enzyme.

Relevant publications from our group:

Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR Nature Communications. 2022, 13: 1927, https://www.nature.com/articles/s41467-022-29423-0

Disulfide-bond-induced structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR J. Am. Chem. Soc. 145 (19), 10700-10711 https://pubs.acs.org/doi/10.1021/jacs.3c01200

Develop MAS NMR techniques and combine them with advanced specific isotope labelling and computational tools for studies of protein dynamics

We combine specific isotope labelling (such as the selective introduction of 1H-13C pairs or 19F) together with sensitive MAS NMR approaches to gain insight into protein dynamics. For example, we have developed MAS NMR methods to bring to light transient states of proteins using relaxation-dispersion methods (which we called “NERRD MAS NMR”). Join the group to develop isotope-labelling, together with our chemistry colleagues, and/or new pulse sequences.

Relevant publications from our group:

The rigid core and flexible surface of amyloid fibrils probed by magic-angle spinning NMR of aromatic residues Angew. Chem. Int. Ed. 2023, e202219314. https://doi.org/10.1002/anie.202219314

Aromatic ring dynamics and excited states detected in a half-megadalton aminopeptidase by specific labeling and MAS NMR J. Am. Chem. Soc., 141 (28), 11183–11195 https://pubs.acs.org/doi/10.1021/jacs.9b04219; highlighted in: https://f1000.com/prime/735988056#eval793563211

Review: Protein dynamics detected by magic-angle spinning relaxation dispersion NMR Current Opinion in Structural Biology 82, 102660 https://doi.org/10.1016/j.sbi.2023.102660

Requirements

Successful candidates shall have a degree in biochemistry or biophysics. At least theoretical knowledge in structural biology research is expected; practical experience in protein production is a plus. We expect candidates to enjoy creative and critical thinking, possess a strong motivation to learn new techniques, solve puzzling questions, and overcome technical challenges.

While the most common route into ISTA’s PhD programme is with a Master degree, candidates holding a relevant BSc degree will also be considered. (See https://phd.pages.ist.ac.at/ for details.)

The environment we offer

Our group is located at IST Austria, at the outskirts of Vienna, one of the cities with highest quality of life according to many rankings. The group was established at ISTA in 2021, and we currently have 9 members from 7 different countries. English is the institute language.

We have access to three brand-new spectrometers (600, 700 and 800 MHz + soon a 400), equipped with either solution-state cryoprobes or MAS NMR probes (0.7 mm to 3.2 mm). We furthermore have access to a state-of-the-art cryo-EM facility and various techniques for protein production and characterisation.

Successful candidates will be offered a competitive salary for up to 5 years.

Applying:

Applications should be sent via ISTA’s graduate school. Details about the application as well as the Graduate School can be found here: https://phd.pages.ista.ac.at/phd-application-admission/

The application deadline is January 8, 2024, and the PhD programme starts in September 2024.

Questions about the NMR projects and informal requests can be addressed to paul.schanda@ist.ac.at

This call is part of IST Austria’s open PhD call 2024 in a wide range of science fields.

Admitted PhD students will have the chance to explore three research groups, which is a unique opportunity to get in contact with e.g. cryo-EM, biophysics, computer sciences or other fields that will enrich your knowledge. Moreover, you will decide only during this rotation period, and many directions stay open to candidates to pursue the PhD.

Please forward this information about ISTA’s PhD programme also to candidates interested in other fields.

Join the virtual open day on Nov 16  https://phd.pages.ist.ac.at/student-open-day/

Find more information here:

The Schanda group: https://ist.ac.at/en/research/schanda-group/

Publications: https://scholar.google.com/citations?hl=en&user=peo3k9EAAAAJ&view_op=list_works&sortby=pubdate

Biochemistry & structural biology at IST Austria: https://biochemistry.pages.ist.ac.at/

IST Austria’s PhD programme: https://phd.ist.ac.at/

The upcoming virtual open day (Nov 16 !): https://phd.pages.ist.ac.at/student-open-day/

Facilities at ISTA: https://ista.ac.at/en/research/scientific-service-units/

Paul Schanda

Institute of Science and Technology Austria

Office: Sunstone I23.O1.009

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https://ist.ac.at/en/research/schanda-group/