Ph.D. students

Tobias Stief (M.Sc. Medizinische Physik)

Katharina Vormann (M.Sc. Biologie)

Mirko Kraus (MSc Biologie)

Sophia Werner (MSc Biologie)

Students

Frederike Nith (BSc Biologie)

• Structural Dynamics and membrane interactions of the SNARE proteins (Collaborators: Prof. Reinhard Jahn, Max Planck Institute for Multidisciplinary Natural Sciences, Göttingen; Dr. Angel Perez-Lara, University of Granada, Spain)

• Characterization of the internal dynamics and the conformational space of intrinsically disordered proteins and of their lipid membrane interactions (Prof. Henrike Heise, IBI-7, Forschungszentrum Jülich; Prof. Birgit Strodel, IBI-7, Forschungszentrum Jülich; Dr. Ralph Biehl, PD Dr. Andreas Stadler, Prof. Stephan Förster, JCNS-1, Forschungszentrum Jülich, Prof. Paolo Carloni, IAS-5 / INM-9, Forschungszentrum Jülich)

• Protein misfolding in neurodegenerative diseases (Jun. Prof. Wolfgang Hoyer, University of Düsseldorf, Prof. Dieter Willbold, University of Düsseldorf and Forschungszentrum Jülich)

• Dynamic binding interactions of the Sars-Cov-2 non structural protein 3 (nsp3) (Prof. Ralf Bartenschlager, German Cancer Research Center (DKFZ), Heidelberg; Prof. Carsten Sachse, ERC-3, Forschungszentrum Jülich)

• Structural dynamics of the plant Ethylen receptor ETR1 (Prof. Georg Groth, University of Düsseldorf; Prof. Holger Gohlke, IAS, Forschungszentrum Jülich)

Stief T., Vormann K., Lakomek N.A., Sensitivity-enhanced NMR ¹⁵N R₁ and R_1ρ relaxation experiments for investigating intrinsically disordered proteins at high magnetic fields, Methods 2024, 223,1-15. DOI: 10.1016/j.ymeth.2024.01.008

Lemke M., Reiners J., Smits S.H.J., Lakomek N., Groth G., Functional reconstitution and structural characterization of the plant hormone receptor ETR1 in lipid nanodiscs, Chem Commun (Camb) 2023; 59(61):9344-9347. DOI: 10.1039/d3cc02619a

Stief, T., Gremer, L., Pribicevic, S., Jahn, R., Perez-Lara, A., Lakomek, N.A., Intrinsic disorder of the SNARE protein SNAP25a in its pre-fusion conformation, J. Mol. Biol.
2023, 435(10), 168069. DOI: 10.1016/j.jmb.2023.168069

Ahlawat S, Mote KR, Lakomek NA, Agarwal V., Solid-State NMR: Methods for Biological Solids, Chem Rev. 2022, 122(10), 9643-9737

Jirasko, V.*, Lends, A.*, Lakomek, N.A.*, Fogeron M.L., Weber M., Malär A., Penzel S., Bartenschlager R., Meier B.H., Böckmann A., Dimer organization of membrane-associated NS5A of hepatitis C virus as determined by highly sensitive ¹H-detected solid-state NMR, Angew. Chem. Int. Ed. Engl. 2021, 60(10), 5339-5347

Lakomek, N.A.^#, Yavuz, H., Jahn, R.^#,Perez-Lara, A.^#, Structural dynamics and transient lipid binding of synaptobrevin-2 tune SNARE assembly and membrane fusion, Proc. Natl. Acad. Sci. 2019, 16(18), 8699-8708.

Lakomek, N.A., Frey, L., Bibow, S., Böckmann, A., Riek, R, Meier, B.H., Proton-detected NMR spectroscopy of nanodisc-embedded membrane proteins: MAS solid-state vs. solution methods, J. Phys. Chem. B 2017, 121(32), 7671-7680.

Lakomek, N.A.*^,#, Draycheva, A.*, Bornemann, T., Wintermeyer, W.^#, Electrostatics and intrinsic disorder drive translocon binding of the SRP receptor FtsY, Angew. Chem. Int. Ed. Engl. 2016, 55(33), 9544-9547.

Lakomek, N.A.^#, Kaufman, J.D., Stahl, J.S., Wingfield, P.T.^#, HIV-1 Envelope Protein gp41: An NMR study of dodecyl phosphocholine embedded gp41 reveals a dynamic prefusion intermediate conformation, Structure 2014, 22(9), 1311-1321.

Lakomek, N.A., Ying, J., Bax, A., Measurement of ¹⁵N relaxation rates in perdeuterated proteins by TROSY-based methods, J. Biomol. NMR 2012, 53, 209-221.

Lange, O.F.*, Lakomek, N.A.*, Farès, C., Schröder, G.F., Walter, K.F.A., Becker, S., Meiler, J., Grubmüller, H., Griesinger, C., de Groot, Bert L., Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution, Science 2008, 320, 1471-1475.

*authors contributed equally