PhD/postdoc in innovative NMR methods – Linser lab

We are looking for an additional group member in the field of NMR spectroscopy on proteins.
Our focus is the characterization of protein structure, dynamics and interactions, using both solution and solid-state NMR spectroscopy. In the past, we have committed ourselves to the development of innovative NMR methodology as well as application of new and established methods to better understand the behavior of various proteins. In particular, we are one of the drivers for proton-detected solid-state NMR methods development, in particular regarding higher-dimensionality experiments and other innovative strategies, improved structure elucidation, and assessment of protein dynamics. Our biological interests are the protein dynamics playing a role for enzymatic function and as well as protein-small molecule and protein/DNA interactions.
The lab has an outstanding infrastructure and research environment, including manifold facilities and services of the MPI for molecular physiology (_expression_, crystallization, etc.) and the IMPRS research school, providing excellent research opportunities. Our lab has an 800 and a 700 MHz high-field NMR spectrometer, a second 800 MHz and a 500 MHz system coming soon, as well as part of the measurement time of a shared 700 MHz system. We use state-of-the-art equipment, including two probes for MAS at 111 kHz. Whereas in the past, most projects were based on solid-state NMR methods, we are now equally applying NMR in solution and in solids with a wide range of facets.

The preferred candidates should be knowledgeable in both, biochemistry and NMR characterization of proteins, including all aspects from protein production, assignments, structure calculation, and basics of dynamics. Applicants should be devoted chemists/biochemists/physicists by training, craving for exciting structural-biology data and leading-edge technical concepts, and foster scientific exchange with their fellow coworkers. A social and committed personality, a high level of detail and strong commitment are also important prerequisites.

Dortmund is a well-connected, diverse, and vibrant city of around 600 k people in Western Germany now with a strong focus on science and education. The group is (and will be) part of a multitude of science platforms fostering high-quality interdisciplinary research and scientific exchange, and most projects involve collaborations with molecular dynamics, drug discovery/medicinal chemistry, and biochemistry groups in the MPI and the department.

If you feel like you meet the above criteria and are interested in developing and applying innovative NMR technology, I would be very happy to get in touch. For PhD applicants, who will be part of the International Max Planck Research School, please note the 18.04.22 as the deadline of the current IMPRS call:
(You would have to apply there, but you are welcome to get in touch with me informally beforehand.)

Please also check the following webpage for more information on the lab:

Some of our recent papers are listed below.

Best regards,
Rasmus Linser

A. Klein, P. Rovó, V. V. Sakhrani, Y. Wang, J. B. Holmes, V. Liu, P. Skowronek, L. Kukuk, S. K. Vasa, P. Güntert, L. J. Mueller, R. Linser, “Atomic-Resolution Chemical Characterization of (2x)72 kDa Tryptophan Synthase via 4D and 5D 1H-Detected Solid-State NMR”, Proc. Natl. Acad. Sci. U.S.A, 119 (4) e2114690119 (2022), DOI: 10.1073/pnas.2114690119 (Link).

A. Klein, S. K. Vasa, B. Söldner, K. Grohe, R. Linser, “Unambiguous Sidechain Assignments for Solid-State Nuclear Magnetic Resonance Structure of Non-deuterated Proteins via a Combined 5D/4D Sidechain-to-Backbone Experiment”, J. Phys. Chem. Lett., 13, 1644–1651 (2022), DOI: 10.1021/acs.jpclett.1c04075 (Link).

H. Singh, C. K. Das S. K. Vasa, K. Grohe, L. V. Schäfer, R. Linser, “The active site of a prototypical “rigid” drug target is marked by extensive conformational dynamics”, Angew. Chem., Int. Ed., 59 (51), 22916-22921(2020), DOI: 10.1002/anie.202009348 (Link).

H. Singh, S. K. Vasa, H. Jangra,  P. Rovó, C. Päslack, C. K. Das, H. Zipse, L. Schäfer, R. Linser, “Fast-microsecond dynamics of the protein-water network in the active site of human carbonic anhydrase II by solid-state NMR spectroscopy.” J. Am. Chem. Soc., 141 (49), 19276-19288, DOI: 10.1021/jacs.9b05311 (2019). (Link)

S. K. Vasa, H. Singh, K.Grohe, R. Linser, "Assessment of a large enzyme-drug complex by proton-detected solid-state NMR without deuteration", Angew. Chem. Int. Ed., 58 (17), 5758-5762, DOI: 10.1002/anie.201811714 (2019). (Link)

P. Rovó, C. A. Smith, D. Gauto, B. L. de Groot, P. Schanda, R. Linser, “Mechanistic insights into microsecond timescale motion of solid proteins using complementary 15N and 1H relaxation dispersion techniques”, J. Am. Chem. Soc., 141 (2), 858–869, DOI: 10.1021/jacs.8b09258 (2019). (Link)

Prof. Dr. Rasmus Linser
Chair for Biomolecular NMR Spectroscopy,
Department of Chemistry and Chemical Biology,
TU Dortmund University,
Otto-Hahn-Str. 4a, 44227 Dortmund