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  • Jirasko, V., Lakomek, N.A., Penzel, S., Fogeron, M.L., Bartenschlager, R., Meier, B.H., Böckmann, A. Proton-detected solid-state NMR of a cell-free synthesized, lipid-reconstituted integral membrane protein, ChemBioChem 2020, doi: 10.1002/cbic.201900765
  • 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.
  • Kumari, P., Frey, L., Sobol, A., Lakomek, N.A., Riek, R., 15N transverse relaxation measurements for the characterization of µs-ms dynamics are deteriorated by the deuterium isotope effect on 15N resulting from solvent exchange, J. Biomol. NMR 2018, 72(3-4), 125-137.
  • Schroeder, S., Kaufman, J.D., Grunwald, M., Walla, P.J., Lakomek, N.A., Wingfield, P.T., HIV-1 gp41 transmembrane oligomerization monitored by FRET and FCS, FEBS Lett. 2018, 592(6), 939-948.
  • Tan, K.O., Agarwal, V., Lakomek, N.A., Penzel,S., Meier, B.H., Ernst, M., Efficient Low-Power TOBSY Sequences for Fast MAS, Solid State Nucl. Magn. Reson. 2018, 89, 27-34.
  • 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., Penzel, S., Lends, A., Cadalbert, R., Ernst, M., Meier, B.H., Microsecond dynamics in ubiquitin probed by solid-state N-15 NMR spectroscopy R relaxation experiments under fast MAS (60–110 kHz), Chem. Eur. J. 2017, 23(39), 9425-9433.
  • Frey, L., Lakomek, N.A., Riek, R., Bibow, S., Micelles vs. bicelles vs. nanodiscs: Comparing the impact of membrane mimetics on membrane protein backbone dynamics, Angew. Chem. Int. Ed. Engl. 2017, 56(1), 380-383.
  • Draycheva, A., Bornemann, T., Lakomek, N.A., Wintermeyer, W., The bacterial SRP receptor, FtsY, is activated on binding to the translocon, Mol. Microbiol. 2016, 02(1), 152-167.
  • 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.
  • Fasshuber, H.K., Lakomek, N.A., Habenstein, B., Loquet, A., Shi, C., Giller, K., Wolff, S., Becker, S., Lange, A., Structural heterogeneity in microcrystalline ubiquitin studied by solid-state NMR., Protein Sci. 2015, 24(5), 592-598.
  • 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., Kaufman J.D., Stahl J.S., Louis J.M., Grishaev A., Wingfield P.T., Bax A., The homotrimeric HIV-1 viral coat protein gp41 shows a high degree of internal dynamics on multiple time scales, Angew. Chem. Int. Ed. Engl. 2013, 52(14), 3911-3915.
  • 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.
  • Ban, D., Funk, M., Gulich, R., Egger, D., Sabo, T. M., Walter, K. F.A., Fenwick, R.B., Giller, K., Pichierri F., de Groot, B.L., Lange, O.F., Grubmüller, H., Salvatella, X., Wolf, M., Loidl, A., Kree, R.#, Stefan, B., Lakomek, N. A., Lee, D., Lunkenheimer, P., Griesinger, C., Kinetics of conformational sampling in ubiquitin and the molecular recognition process, Angew. Chem Int. Ed. 2011, 50(48), 11437-11440.
  • Fenwick, R.B., Esteban-Martín, S., Richter, B., Lee, D., Walter, K.F.A., Milanovic, D., Becker, S., Lakomek, N.A., Griesinger, C., Salvatella, X., Weak long-range correlated motions in a surface patch of ubiquitin involved in molecular recognition, J. Am. Chem. Soc. 2011, 133(27), 10336-10339.
  • Farès, C., Lakomek, N.A., Walter, K.F., Frank, B.T., Meiler, J., Becker, S., Griesinger, C., Accessing ns-microsecond side chain dynamics in ubiquitin with methyl RDCs., J. Biomol. NMR 2009, 45(1-2), 23-44.
  • Friedland, G.D., Lakomek, N.A., Griesinger, C., Meiler, J., Kortemme, T., A correspondence between solution-state dynamics of an individual protein and the sequence and conformational diversity of its family, PloS Comput. Biol. 2009, e1000393. Epub 2009 May 29.
  • Salmon, L., Bouvignies, G., Markwick, P., Lakomek, N., Showalter, S., Li, K.W., Walter, K., Griesinger, C., Brüschweiler, R., Blackledge, M., Protein conformational flexibility from structure-free analysis of NMR dipolar couplings: quantitative and absolute determination of backbone motion in ubiquitin, Angew. Chem. Intl. Ed. Engl. 2009, 48(23), 4154-4157.
  • Lakomek, N.A., Lange, O.F., Walter, K.F.A., Farès, C., Egger, D., Lunkenheimer, P., Meiler, J., Grubmüller, H., Becker, S., de Groot, B.L., Griesinger, C., Residual dipolar couplings as a tool to study molecular recognition of ubiquitin, Biochem. Soc. Trans. 2008, 36, 1433-1437.
  • Lakomek, N.A., New methods in NMR spectroscopy for the study of protein dynamics, PhD thesis, 2008, University of Göttingen, Germany
  • 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.
  • Lakomek, N. A., Walter, K. F. A., Farès, C., Lange, O. F., de Groot, B. L., Grubmüller, H., Brüschweiler, R., Munk, A., Becker, S., Meiler, J., Griesinger, C., Self-consistent residual dipolar coupling based model-free analysis for the robust determination of nanosecond to microsecond protein dynamics, J. Biomol. NMR 2008, 41, 139-115.
  • Lakomek, N. A., Carlomagno, T., Becker, S., Griesinger, C., Meiler, J., A thorough dynamic interpretation of residual dipolar couplings in ubiquitin, J. Biomol. NMR 2006, 34, 101-115.
  • Lakomek, N. A., Fares, C., Becker, S., Carlomagno, T., Meiler, J., Griesinger, C., Side-chain orientation and hydrogen-bonding imprint supra-c motion on the protein backbone of ubiquitin, Angew. Chem. Int. Ed. Engl. 2005, 44, 7776-7778.
  • Razeto, A., Ramakrishnan, V., Litterst, C.M., Giller, K., Griesinger, C., Carlomagno, T., Lakomek, N., Heimburg, T., Londrini, M., Pfitzner, E., Becker, S., Structure of the NCoA-1/SRC-1 PAS-B domain bound to LXXLL motif of the STAT6 transactivation domain, J. Mol. Biol. 2004, 336, 319-329.
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