NMR-basierte strukturelle Chemie

Um neue Arzneimittel gegen Infektionskrankheiten entwickeln zu können, müssen wir die molekularen Grundlagen entdecken. Daher ist es notwendig zu verstehen, wie der Replikationsvorgang der Erreger abläuft, welche Wechselwirkungen zwischen Erreger und Wirtszelle stattfinden und wie diese Vorgänge reguliert werden. Die Forschungsgruppe NMR-basierte Strukturbiologie untersucht RNA-Protein-Komplexe, die an verschiedenen Stellen der Infektion beteiligt sind, auf Seiten des Lebenszyklus sowohl des Erregers als auch der Wirtszelle.



A. Graziadei, P. Masiewicz, A. Lapinaite, T. Carlomagno Archaea box C/D enzymes methylate two distinct substrate rRNA sequences with different efficiency. RNA 2016, in Press, DOI: no DOI available

S. Kozak, L. Lercher, M. N. Karanth, M. Peter, S. Gael, J. Márquez, R. Meijers, T. Carlomagno*, S. Boivin Optimization of protein samples for NMR using thermal shift assays. Submitted, DOI: no DOI available


Bowman A, Lercher L, Singh HR, Zinne D, Timinszky G, Carlomagno T, Ladurner AG The histone chaperone sNASP binds a conserved peptide motif within the globular core of histone H3 through its TPR repeats. Nucleic Acid Res. 2015 Sep 15; eprint DOI: link

Wollrab E, Scherer S, Aubriet F, Carre V, Carlomagno T, Codutti L, Ott A Chemical Analysis of a "Miller-Type" Complex Prebiotic Broth : Part I: Chemical Diversity, Oxygen and Nitrogen Based Polymers. Orig Life Evol Biosph 2015 Oct 27; eprint DOI: link

Onila I, ten Brink T, Fredriksson K, Codutti L, Mazur A, Griesinger C, Carlomagno T, Exner TE On-the-Fly Integration of Data from a Spin-Diffusion-Based NMR Experiment into Protein-Ligand Docking. J Chem Inf Model. 2015 Sep 28;55(9):1962-72. doi: link

Codutti L, Leppek K, Zalesak J, Windeisen V, Masiewicz P, Stoecklin G, Carlomagno T A Distinct, Sequence-Induced Conformation Is Required for Recognition of the Constitutive Decay Element RNA by Roquin. Structure. 2015 Aug 4;23(8):1437-47. doi: link

Simon B, Masiewicz P, Ephrussi A, Carlomagno T The structure of the SOLE element of oskar mRNA. RNA. 2015 Aug;21(8):1444-53. doi: link

J. Sikorska, L. Codutti, L. Skjærven, B. Elshorst, R. Saez-Ameneiro, A. Angelini, P. Monecke, T. Carlomagno Identification of new scaffolds with INPHARMA-based virtual screening. Med Chem Com 2015(6):1501-07. doi: link

Marchanka A, Simon B, Althoff-Ospelt G, Carlomagno T RNA structure determination by solid-state NMR spectroscopy. Nat Commun. 2015 May 11;6:7024. doi: link


A. Marchanka T. Carlomagno Solid-state NMR and RNA Structure: A new Partnership? eMagRes 2014 3, 119–128. doi: link

Bock T, Chen WH, Ori A, Malik N, Silva-Martin N, Huerta-Cepas J, Powell ST, Kastritis PL, Smyshlyaev G, Vonkova I, Kirkpatrick J, Doerks T, Nesme L, Baßler J, Kos M, Hurt E, Carlomagno T, Gavin AC, Barabas O, Müller CW, van Noort V, Beck M, Bork P. An integrated approach for genome annotation of the eukaryotic thermophile Chaetomium thermophilum. Nucleic Acids Res. 42(22):13525-13533. doi:10.1093/nar/gku1147 Europe PMC | doi

Findeisen P, Mühlhausen S, Dempewolf S, Hertzog J, Zietlow A, Carlomagno T, Kollmar M. Six subgroups and extensive recent duplications characterize the evolution of the eukaryotic tubulin protein family Genome Biol Evol 6(9):2274-2288. doi:10.1093/gbe/evu187 Europe PMC | doi

Carlomagno T. (2014) Present and future of NMR for RNA-protein complexes: a perspective of integrated structural biology J. Magn. Reson. 241:126-136. doi:10.1016/j.jmr.2013.10.007 Europe PMC | doi

Canales A, Nieto L, Rodríguez-Salarichs J, Sánchez-Murcia PA, Coderch C, Cortés-Cabrera A, Paterson I, Carlomagno T, Gago F, Andreu JM, Altmann KH, Jiménez-Barbero J, Díaz JF. Molecular recognition of epothilones by microtubules and tubulin dimers revealed by biochemical and NMR approaches. ACS Chem. Biol. 9(4):1033-1043. doi:10.1021/cb400673h Europe PMC | doi


Lapinaite A, Simon B, Skjaerven L, Rakwalska-Bange M, Gabel F, Carlomagno T. The structure of the box C/D enzyme reveals regulation of RNA methylation. Nature 502(7472):519-523. doi:10.1038/nature12581 Europe PMC | doi

Schulte B, John I, Simon B, Brockmann C, Oelmeier SA, Jahraus B, Kirchgessner H, Riplinger S, Carlomagno T, Wabnitz GH, Samstag Y. A reducing milieu renders cofilin insensitive to phosphatidylinositol 4,5-bisphosphate (PIP2) inhibition. J. Biol. Chem. 288(41):29430-29439. doi:10.1074/jbc.m113.479766 Europe PMC | doi

Marchanka A, Simon B, Carlomagno T. A suite of solid-state NMR experiments for RNA intranucleotide resonance assignment in a 21 kDa protein-RNA complex. Angew. Chem. Int. Ed. Engl. 52(38):9996-10001. doi:10.1002/anie.201304779 Europe PMC | doi

Skjærven L, Codutti L, Angelini A, Grimaldi M, Latek D, Monecke P, Dreyer MK, Carlomagno T. Accounting for conformational variability in protein-ligand docking with NMR-guided rescoring. J. Am. Chem. Soc. 135(15):5819-5827. doi:10.1021/ja4007468 Europe PMC | doi

Carlomagno T, Amata I, Codutti L, Falb M, Fohrer J, Masiewicz P, Simon B. Structural principles of RNA catalysis in a 2'-5' lariat-forming ribozyme. J. Am. Chem. Soc. 135(11):4403-4411. doi:10.1021/ja311868t Europe PMC | doi

Asami S, Rakwalska-Bange M, Carlomagno T, Reif B. Protein-RNA interfaces probed by 1H-detected MAS solid-state NMR spectroscopy. Angew. Chem. Int. Ed. Engl. 52(8):2345-2349. doi:10.1002/anie.201208024 Europe PMC | doi

Latek D, Pasznik P, Carlomagno T, Filipek S. Towards improved quality of GPCR models by usage of multiple templates and profile-profile comparison. PLoS ONE 8(2):e56742. doi:10.1371/journal.pone.0056742 Europe PMC | doi


Ballaré C, Lange M, Lapinaite A, Martin GM, Morey L, Pascual G, Liefke R, Simon B, Shi Y, Gozani O, Carlomagno T, Benitah SA, Di Croce L. Phf19 links methylated Lys36 of histone H3 to regulation of Polycomb activity. Nat. Struct. Mol. Biol. 19(12):1257-1265. doi:10.1038/nsmb.2434 Europe PMC | doi

Persch E, Basile T, Bockelmann S, Huss M, Wieczorek H, Carlomagno T, Menche D. Synthesis and biological evaluation of a water-soluble derivative of the potent V-ATPase inhibitor archazolid. Bioorg. Med. Chem. Lett. 22(24):7735-7738. doi:10.1016/j.bmcl.2012.09.081 Europe PMC | doi

Stauch B, Orts J, Carlomagno T. The description of protein internal motions aids selection of ligand binding poses by the INPHARMA method. J. Biomol. NMR 54(3):245-256. doi:10.1007/s10858-012-9662-1 Europe PMC | doi

Dreisigacker S, Latek D, Bockelmann S, Huss M, Wieczorek H, Filipek S, Gohlke H, Menche D, Carlomagno T. Understanding the inhibitory effect of highly potent and selective archazolides binding to the vacuolar ATPase. J Chem Inf Model 52(8):2265-2272. doi:10.1021/ci300242d Europe PMC | doi

Carlomagno T. NMR in natural products: understanding conformation, configuration and receptor interactions. Nat Prod Rep 29(5):536-554. doi:10.1039/c2np00098a Europe PMC | doi

Lee Y, Zeng H, Mazur A, Wegstroth M, Carlomagno T, Reese M, Lee D, Becker S, Griesinger C, Hilty C. Hyperpolarized binding pocket nuclear Overhauser effect for determination of competitive ligand binding. Angew. Chem. Int. Ed. Engl. 51(21):5179-5182. doi:10.1002/anie.201201003 Europe PMC | doi

Orts J, Bartoschek S, Griesinger C, Monecke P, Carlomagno T. An NMR-based scoring function improves the accuracy of binding pose predictions by docking by two orders of magnitude. J. Biomol. NMR 52(1):23-30. doi:10.1007/s10858-011-9590-5 Europe PMC | doi


Corradi V, Mancini M, Santucci MA, Carlomagno T, Sanfelice D, Mori M, Vignaroli G, Falchi F, Manetti F, Radi M, Botta M. Computational techniques are valuable tools for the discovery of protein-protein interaction inhibitors: the 14-3-3σ case. Bioorg. Med. Chem. Lett. 21(22):6867-6871. doi:10.1016/j.bmcl.2011.09.011 Europe PMC | doi

Simon B, Kirkpatrick JP, Eckhardt S, Reuter M, Rocha EA, Andrade-Navarro MA, Sehr P, Pillai RS, Carlomagno T. Recognition of 2'-O-methylated 3'-end of piRNA by the PAZ domain of a Piwi protein. Structure 19(2):172-180. doi:10.1016/j.str.2010.11.015 Europe PMC | doi


Dervillez X, Klaukien V, Dürr R, Koch J, Kreutz A, Haarmann T, Stoll M, Lee D, Carlomagno T, Schnierle B, Möbius K, Königs C, Griesinger C, Dietrich U. Peptide ligands selected with CD4-induced epitopes on native dualtropic HIV-1 envelope proteins mimic extracellular coreceptor domains and bind to HIV-1 gp120 independently of coreceptor usage. J. Virol. 84(19):10131-10138. doi:10.1128/jvi.00165-10

Falb M, Amata I, Gabel F, Simon B, Carlomagno T. Structure of the K-turn U4 RNA: a combined NMR and SANS study. Nucleic Acids Res. 38(18):6274-6285. doi:10.1093/nar/gkq380

Kumar A, Heise H, Blommers MJ, Krastel P, Schmitt E, Petersen F, Jeganathan S, Mandelkow EM, Carlomagno T, Griesinger C, Baldus M. Interaction of epothilone B (patupilone) with microtubules as detected by two-dimensional solid-state NMR spectroscopy. Angew. Chem. Int. Ed. Engl. 49(41):7504-7507. doi:10.1002/anie.201001946

Bülow L, Nickeleit I, Girbig AK, Brodmann T, Rentsch A, Eggert U, Sasse F, Steinmetz H, Frank R, Carlomagno T, Malek NP, Kalesse M. Synthesis and biological characterization of argyrin F. ChemMedChem 5(6):832-836. doi:10.1002/cmdc.201090023

Erdélyi M, Navarro-Vázquez A, Pfeiffer B, Kuzniewski CN, Felser A, Widmer T, Gertsch J, Pera B, Díaz JF, Altmann KH, Carlomagno T. The binding mode of side chain- and C3-modified epothilones to tubulin. ChemMedChem 5(6):911-920. doi:10.1002/cmdc.201000050

Kubicek K, Grimm SK, Orts J, Sasse F, Carlomagno T. The tubulin-bound structure of the antimitotic drug tubulysin. Angew. Chem. Int. Ed. Engl. 49(28):4809-4812. doi:10.1002/anie.200906828

Stauch B, Simon B, Basile T, Schneider G, Malek NP, Kalesse M, Carlomagno T. Elucidation of the structure and intermolecular interactions of a reversible cyclic-peptide inhibitor of the proteasome by NMR spectroscopy and molecular modeling. Angew. Chem. Int. Ed. Engl. 49(23):3934-3938. doi:10.1002/anie.201000140

Rodríguez-Castañeda F, Coudevylle N, Becker S, Brose N, Carlomagno T, Griesinger C. 1H, 13C and 15N resonance assignments of the Calmodulin-Munc13-1 peptide complex. Biomol NMR Assign 4(1):45-48. doi:10.1007/s12104-009-9204-2

Jehle S, Falb M, Kirkpatrick JP, Oschkinat H, van Rossum BJ, Althoff G, Carlomagno T. Intermolecular protein-RNA interactions revealed by 2D 31P-15N magic angle spinning solid-state NMR spectroscopy. J. Am. Chem. Soc. 132(11):3842-3846. doi:10.1021/ja909723f

Bartoschek S, Klabunde T, Defossa E, Dietrich V, Stengelin S, Griesinger C, Carlomagno T, Focken I, Wendt KU. Drug design for G-protein-coupled receptors by a ligand-based NMR method. Angew. Chem. Int. Ed. Engl. 49(8):1426-1429. doi:10.1002/anie.200905102

Rodríguez-Castañeda F, Maestre-Martínez M, Coudevylle N, Dimova K, Junge H, Lipstein N, Lee D, Becker S, Brose N, Jahn O, Carlomagno T, Griesinger C. Modular architecture of Munc13/calmodulin complexes: dual regulation by Ca2+ and possible function in short-term synaptic plasticity. EMBO J. 29(3):680-691. doi:10.1038/emboj.2009.373


Orts J, Griesinger C, Carlomagno T. The INPHARMA technique for pharmacophore mapping: A theoretical guide to the method. J. Magn. Reson. 200(1):64-73. doi:10.1016/j.jmr.2009.06.006

Li P, Kirkpatrick J, Carlomagno T. An efficient strategy for the determination of the three-dimensional architecture of ribonucleoprotein complexes by the combination of a few easily accessible NMR and biochemical data: intermolecular recognition in a U4 spliceosomal complex. J. Mol. Biol. 388(2):283-298. doi:10.1016/j.jmb.2009.03.001

Kirkpatrick JP, Li P, Carlomagno T. Probing mutation-induced structural perturbations by refinement against residual dipolar couplings: application to the U4 spliceosomal RNP complex. Chembiochem 10(6):1007-1014. doi:10.1002/cbic.200800786


Carlomagno T, Amata I, Williamson JR, Hennig M. NMR assignments of HIV-2 TAR RNA. Biomol NMR Assign 2(2):167-169. doi:10.1007/s12104-008-9112-x

Nickeleit I, Zender S, Sasse F, Geffers R, Brandes G, Sörensen I, Steinmetz H, Kubicka S, Carlomagno T, Menche D, Gütgemann I, Buer J, Gossler A, Manns MP, Kalesse M, Frank R, Malek NP. Argyrin a reveals a critical role for the tumor suppressor protein p27(kip1) in mediating antitumor activities in response to proteasome inhibition. Cancer Cell 14(1):23-35. doi:10.1016/j.ccr.2008.05.016

Erdélyi M, Pfeiffer B, Hauenstein K, Fohrer J, Gertsch J, Altmann KH, Carlomagno T. Conformational preferences of natural and C3-modified epothilones in aqueous solution. J. Med. Chem. 51(5):1469-1473. doi:10.1021/jm7013452

Höfer P, Parigi G, Luchinat C, Carl P, Guthausen G, Reese M, Carlomagno T, Griesinger C, Bennati M. Field dependent dynamic nuclear polarization with radicals in aqueous solution. J. Am. Chem. Soc. 130(11):3254-3255. doi:10.1021/ja0783207

Farès C, Hassfeld J, Menche D, Carlomagno T. Simultaneous determination of the conformation and relative configuration of archazolide a by using nuclear overhauser effects, J couplings, and residual dipolar couplings. Angew. Chem. Int. Ed. Engl. 47(20):3722-3726. doi:10.1002/anie.200800225

Hofer P, Carl P, Guthausen G, Prisner T, Reese M, Carlomagno T, Griesinger C, Bennati M. Studies of dynamic nuclear polarization with nitroxides in aqueous solution. Appl Magn Reson 34(3-4):393-398.

Orts J, Grimm SK, Griesinger C, Wendt KU, Bartoschek S, Carlomagno T. Specific methyl group protonation for the measurement of pharmacophore-specific interligand NOE interactions. Chemistry 14(25):7517-7520. doi:10.1002/chem.200800880

Orts J, Tuma J, Reese M, Grimm SK, Monecke P, Bartoschek S, Schiffer A, Wendt KU, Griesinger C, Carlomagno T. Crystallography-independent determination of ligand binding modes. Angew. Chem. Int. Ed. Engl. 47(40):7736-7740. doi:10.1002/anie.200801792

Reese M, Lennartz D, Marquardsen T, Hofer P, Tavernier A, Carl P, Schippmann T, Bennati M, Carlomagno T, Engelke F, Griesinger C. Construction of a liquid-state NMR DNP shuttle spectrometer: First experimental results and evaluation of optimal performance characteristics. Appl Magn Reson 34(3-4):301-311.


Farès C, Amata I, Carlomagno T. 13C-detection in RNA bases: revealing structure-chemical shift relationships. J. Am. Chem. Soc. 129(51):15814-15823. doi:10.1021/ja0727417

Lange A, Schupp T, Petersen F, Carlomagno T, Baldus M. High-resolution solid-state NMR structure of an anticancer agent. ChemMedChem 2(4):522-527. doi:10.1002/cmdc.200600299

Liu S, Li P, Dybkov O, Nottrott S, Hartmuth K, Lührmann R, Carlomagno T, Wahl MC. Binding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNP. Science 316(5821):115-120. doi:10.1126/science.1137924

Carlomagno T, Baldus M, Griesinger C. Bio-nuclear magnetic resonance. doi:10.1016/b0-08-045044-x/00095-x

Reese M, Sánchez-Pedregal VM, Kubicek K, Meiler J, Blommers MJ, Griesinger C, Carlomagno T. Structural basis of the activity of the microtubule-stabilizing agent epothilone a studied by NMR spectroscopy in solution. Angew. Chem. Int. Ed. Engl. 46(11):1864-1868. doi:10.1002/anie.200604505


Sánchez-Pedregal VM, Kubicek K, Meiler J, Lyothier I, Paterson I, Carlomagno T. The tubulin-bound conformation of discodermolide derived by NMR studies in solution supports a common pharmacophore model for epothilone and discodermolide. Angew. Chem. Int. Ed. Engl. 45(44):7388-7394. doi:10.1002/anie.200602793

Fohrer J, Reinscheid U, Hennig M, Carlomagno T. Calculation of the dependence of homo- and heteronuclear 3J and 2J scalar couplings for the determination of the 2'-hydroxy conformation in RNA. Angew. Chem. Int. Ed. Engl. 45(42):7033-7036. doi:10.1002/anie.200602583

Hassfeld J, Farès C, Steinmetz H, Carlomagno T, Menche D. Stereochemical determination of Archazolid A and B, highly potent vacuolar-type ATPase inhibitors from the Myxobacterium Archangium gephyra. Org. Lett. 8(21):4751-4754. doi:10.1021/ol061831y

Farès C, Carlomagno T. SHARP-TACSY: triple-band tailored correlated spectroscopy for base-to-sugar transfer in nucleic acid residues with intermediate time scale motions. J. Am. Chem. Soc. 128(30):9856-9862. doi:10.1021/ja061424h

Fohrer J, Hennig M, Carlomagno T. Influence of the 2'-hydroxyl group conformation on the stability of A-form helices in RNA. J. Mol. Biol. 356(2):280-287. doi:10.1016/j.jmb.2005.11.043

Lakomek NA, Carlomagno T, Becker S, Griesinger C, Meiler J. A thorough dynamic interpretation of residual dipolar couplings in ubiquitin. J. Biomol. NMR 34(2):101-115. doi:10.1007/s10858-005-5686-0

Carlomagno T, Griesinger C. Transferred Cross-Correlated Relaxation: Application to Drug/Target Complexes. doi:10.1007/1-4020-3910-7_134

Raghunathan D, Sánchez-Pedregal VM, Junker J, Schwiegk C, Kalesse M, Kirschning A, Carlomagno T. TAR-RNA recognition by a novel cyclic aminoglycoside analogue. Nucleic Acids Res. 34(12):3599-3608. doi:10.1093/nar/gkl494


Lakomek NA, Farès C, Becker S, Carlomagno T, Meiler J, Griesinger C. Side-chain orientation and hydrogen-bonding imprint supra-Tau(c) motion on the protein backbone of ubiquitin. Angew. Chem. Int. Ed. Engl. 44(47):7776-7778. doi:10.1002/anie.200502573

Sánchez-Pedregal VM, Reese M, Meiler J, Blommers MJ, Griesinger C, Carlomagno T. The INPHARMA method: protein-mediated interligand NOEs for pharmacophore mapping. Angew. Chem. Int. Ed. Engl. 44(27):4172-4175. doi:10.1002/anie.200500503

Verdier L, Al-Sabi A, Rivier JE, Olivera BM, Terlau H, Carlomagno T. Identification of a novel pharmacophore for peptide toxins interacting with K+ channels. J. Biol. Chem. 280(22):21246-21255. doi:10.1074/jbc.m502376200

Hennig M, Fohrer J, Carlomagno T. Assignment and NOE analysis of 2'-hydroxyl protons in RNA: implications for stabilization of RNA A-form duplexes. J. Am. Chem. Soc. 127(7):2028-2029. doi:10.1021/ja043390o

Carlomagno T. Ligand-target interactions: what can we learn from NMR? Annu Rev Biophys Biomol Struct 34:245-266. doi:10.1146/annurev.biophys.34.040204.144419


Al-Sabi A, Lennartz D, Ferber M, Gulyas J, Rivier JE, Olivera BM, Carlomagno T, Terlau H. KappaM-conotoxin RIIIK, structural and functional novelty in a K+ channel antagonist. Biochemistry 43(27):8625-8635. doi:10.1021/bi0495681

Razeto A, Ramakrishnan V, Litterst CM, Giller K, Griesinger C, Carlomagno T, Lakomek N, Heimburg T, Lodrini M, Pfitzner E, Becker S. Structure of the NCoA-1/SRC-1 PAS-B domain bound to the LXXLL motif of the STAT6 transactivation domain. J. Mol. Biol. 336(2):319-329. doi:10.1016/j.jmb.2003.12.057


Carlomagno T, Bermel W, Griesinger C. Measuring the chi 1 torsion angle in protein by CH-CH cross-correlated relaxation: a new resolution-optimised experiment. J. Biomol. NMR 27(2):151-157. doi:10.1023/a:1024927527767

Kipping M, Lilie H, Lindenstrauss U, Andreesen JR, Griesinger C, Carlomagno T, Brüser T. Structural studies on a twin-arginine signal sequence. FEBS Lett. 550(1-3):18-22. doi:10.1016/s0014-5793(03)00804-4

Carlomagno T, Blommers MJ, Meiler J, Jahnke W, Schupp T, Petersen F, Schinzer D, Altmann KH, Griesinger C. The high-resolution solution structure of epothilone A bound to tubulin: an understanding of the structure-activity relationships for a powerful class of antitumor agents. Angew. Chem. Int. Ed. Engl. 42(22):2511-2515. doi:10.1002/anie.200351276

Carlomagno T, Sánchez VM, Blommers MJ, Griesinger C. Derivation of dihedral angles from CH-CH dipolar-dipolar cross-correlated relaxation rates: a C-C torsion involving a quaternary carbon atom in epothilone A bound to tubulin. Angew. Chem. Int. Ed. Engl. 42(22):2515-2517. doi:10.1002/anie.200350950


Carlomagno T, Hennig M, Williamson JR. A novel PH-cT-COSY methodology for measuring JPH coupling constants in unlabeled nucleic acids. application to HIV-2 TAR RNA. J. Biomol. NMR 22(1):65-81. doi:10.1023/a:1013811631477


Carlomagno T, Blommers MJ, Meiler J, Cuenoud B, Griesinger C. Determination of aliphatic side-chain conformation using cross-correlated relaxation: application to an extraordinarily stable 2'-aminoethoxy-modified oligonucleotide triplex. J. Am. Chem. Soc. 123(30):7364-7370. doi:10.1021/ja002592r

Hennig M, Carlomagno T, Williamson JR. Residual dipolar coupling TOCSY for direct through space correlations of base protons and phosphorus nuclei in RNA. J. Am. Chem. Soc. 123(14):3395-3396. doi:10.1021/ja005835o

Carlomagno T, Prasch T, Glaser SNJ. COIN TACSY, a novel approach to tailored correlation spectroscopy. J. Magn. Reson. 149(1):52-57.

Schwalbe H, Carlomagno T, Hennig M, Junker J, Reif B, Richter C, Griesinger C. Cross-correlated relaxation for measurement of angles between tensorial interactions. Meth. Enzymol. 338:35-81. doi:10.1016/s0076-6879(02)38215-6


Carlomagno T, Griesinger C. Errors in the measurement of cross-correlated relaxation rates and how to avoid them. J. Magn. Reson. 144(2):280-287. doi:10.1006/jmre.2000.2056

Carlomagno T, Peti W, Griesinger C. A new method for the simultaneous measurement of magnitude and sign of 1DCH and 1DHH dipolar couplings in methylene groups. J. Biomol. NMR 17(2):99-109. doi:10.1023/a:1008346902500

Carlomagno T, Maurer M, Hennig M, Griesinger C. Ubiquitin backbone motion studied via NHN−C‘Cα dipolar−dipolar and C‘−C‘Cα/NHN CSA−dipolar cross-correlated relaxation. J. Am. Chem. Soc. 122(21):5105-5113.


Carlomagno T, Felli IC, Czech M, Fischer R, Sprinzl M, Griesinger C. Transferred cross-correlated relaxation: application to the determination of sugar pucker in an aminoacylated tRNA-mimetic weakly bound to EF-Tu. J. Am. Chem. Soc. 121(9):1945-1948.


Carlomagno T, Schwalbe H, Rexroth A, Sorensen OW, Griesinger C. New methylene specific experiments for the measurement of scalar spin-spin coupling constants between protons attached to 13C. J. Magn. Reson. 135(1):216-226. doi:10.1006/jmre.1998.1545


Carlomagno T, Luy B, Glaser SJ. "Kin " HEHAHA Sequences, Heteronuclear Hartmann-Hahn Transfer with Different Bandwidths for Spins I and S. J. Magn. Reson. 126(1):110-119. doi:10.1006/jmre.1997.1157

Carlomagno T, Mantile G, Bazzo R, Miele L, Paolillo L, Mukherjee AB, Barbato G. Resonance assignment and secondary structure determination and stability of the recombinant human uteroglobin with heteronuclear multidimensional NMR. J. Biomol. NMR 9(1):35-46. doi:10.1023/a:1018619501038


Carlomagno T, Maurer M, Sattler M, Schwendinger MG, Glaser SJ, Griesinger C. PLUSH TACSY: Homonuclear planar TACSY with two-band selective shaped pulses applied to C(α),C' transfer and C (β),C (aromatic) correlations. J. Biomol. NMR 8(2):161-170. doi:10.1007/bf00211162


Benedetti E, Carlomagno T, Fraternali F, Hamada Y, Hayashi K, Paolillo L, Shioiri T. Conformational analysis of dolastatin 10: an NMR and theoretical approach. Biopolymers 36(4):525-538. doi:10.1002/bip.360360414


  • Prof. Dr. Teresa Carlomagno

    Leiterin der Arbeitsgruppe

    0531 6181-7300