Post-doc position Biomolecular MAS-/solution-NMR of protein dynamics

Post-doc positions are open in the Schanda group at the Institute of Science and Technology Austria (ISTA)

We welcome applications for joining our dynamic international team and working on exciting questions of protein dynamics and function, using and developing NMR in combination with other techniques.

Several projects are currently available, as briefly described below. The positions have some flexibility, and we welcome candidates interested in a range of techniques, from developing new NMR approaches to study protein dynamics to biological questions where NMR and other techniques are used as tools to decipher biological mechanisms, e.g.:

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. We study the import machinery, and decipher the dynamics and interactions important for importing proteins, of for removing 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.

Enzyme dynamics and allostery

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. We combine solution- and MAS NMR to zoom into the dynamic coupling that underlies allostery, and how mutations that occurred along evolution modify dynamics and function.

Develop and apply MAS NMR to study how dynamics underlies protein function

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. Ongoing projects combine specific isotope labelling with new NMR pulse sequences to gain more detailed insight into motions.

Relevant publications from our group:

Chaperones & mitochondria

Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space. Cell 175(5): 1365-1379; highlighted in

Architecture and assembly dynamics of the essential mitochondrial chaperone complex TIM9·10·12. Structure2021, 29: 1-9.

Structural basis of client specificity in mitochondrial membrane-protein chaperones., Science Advances. 2020, 6, 51: eabd0263 ,

Structural Investigation of a 1 MDa Chaperonin in Action. Science Advances, 4, eaau4196

Dynamics in large assemblies

Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR Nature Communications. 2022, 13: 1927,

Disulfide-bond-induced structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR J. Am. Chem. Soc. 145 (19), 10700-10711

Mechanism of the allosteric activation of the ClpP protease machinery by active-site inhibitors. Sci. Adv., 5 (9), eaaw3818

MAS NMR methods development & dynamics studies

The rigid core and flexible surface of amyloid fibrils probed by magic-angle spinning NMR of aromatic residues Angew. Chem. Int. Ed. 2023, e202219314.

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; highlighted in:

Review: Protein dynamics detected by magic-angle spinning relaxation dispersion NMR Current Opinion in Structural Biology 82, 102660


Successful candidates shall have a PhD degree in biochemistry or biophysics, and ideally experience in NMR spectroscopy applied to biomolecules. A strong background in structural biology and protein production and/or bio-NMR methods development is expected. Successful candidates enjoy creative and critical thinking, possess a strong motivation to learn new techniques, solve puzzling questions, and overcome technical challenges.

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.

Our institute is rapidly growing, and you will have the chance to be exposed to a wide range of research areas (with many joint seminars), and with several new faculty joining our structural biology programme in 2024, you will have a chance to connect to a community including cryo-EM, electron tomography, machine learning, protein design, many groups working in developmental, cellular and molecular biology,… We believe it is a highly stimulating environment for a young researcher on an academic career track.

The post-doc contract can be up to 5 years, allowing candidates to develop not only their skills but also prepare for positioning themselves on their way to an academic career.


Please send your appliction, including

* a detailed letter that describes your background and motivations/reasons for applying as well as your vision for your research

* your publication record, possibly your experience in supervision of students, presentations,...

* names of 2-3 references


Find more information here:

The Schanda group:


Biochemistry & structural biology at IST Austria:

IST Austria’s PhD programme:

Facilities at ISTA:

Paul Schanda

Institute of Science and Technology Austria

Office: Sunstone I23.O1.009