53. Reddy, J., Pratihar, S., Ban, D., Frischkorn, S., Becker, S., Griesinger, C., Lee, D.: Simultaneous determination of fast and slow dynamics in molecules using extreme CPMG relaxation dispersion experiments. J. Biomol. NMR, [In-Press]

52. Trigo-Mouriño, P., Griesinger, C., Lee, D.: Label-free NMR-based dissociation kinetics determination. J. Biomol. NMR, [In-Press]

51. Khan, N., Ban, D., Trigo-Mourino, P., Konrad, M., Lee, D., Sabo, T.M.: 1H, 13C and 15N resonance assignment of human guanylate kinase. Biomol. NMR Assign. 2017, [In-Press]

50. Ikeya, T., Ban, D., Lee, D., Ito, Y., Kato, K., Griesinger, C.: Solution NMR views of dynamical ordering of biomacromolecules. Biochim. Biophys. Acta. 2017, [In-Press]

49. Ban, D., Smith, C. A., de Groot, B.L., Griesinger, C., Lee, D.: Recent advances in measuring the kinetics of biomolecules by NMR relaxation dispersion spectroscopy. Arch. Biochem. Biophys. 2017, 628, 81-91.


48. Partihar, S., Sabo, T.M., Ban, D., Fenwick, R.B., Becker, S., Salvatella, X., Griesinger, C., Lee, D.: Kinetics of the antibody recognition site in the third IgG-binding domain of protein G. Angew. Chem. Int. Ed. 2016, 55, 9567-9570.

47. Chakrabarti, K.S., Ban, D., Partihar, S., Reddy, J.G., Becker, S., Griesinger, C., Lee, D.: High-power 1H composite pulse decoupling provides artifact free exchange-mediated saturation transfer (EST) experiments. J. Magn. Reson. 2016, 269, 65-69.

46. Smith, C.A., Ban, D., Pratihar, S., Giller, K., Paulat, M., Becker, S., Griesinger, C., Lee, D., de Groot, B.L.: Allosteric switch regulates protein-protein binding through collective motion. Proc. Nat. Acad. Sci. 2016, 113, 3269-3274.


45. Carneiro, M.G., Reddy, J.G., Griesinger, C., Lee, D.: Speeding-up exchange-mediated saturation transfer experiments by Fourier transform. J. Biomol. NMR 2015, 63, 237-244.

44. Sabo, T.M., Trent, J.O., Lee, D.: Population shuffling between ground and high energy excited states. Protein Sci. 2015, 24, 1714-1719.

43. Pilger, J., Mazur, A., Monecke, P., Schreuder, H., Elshorst, B., Bartoschek, S., Langer, T., Schiffer, A., Krimm, I., Wegstroth, M., Lee, D., Hessler, G., Wendt, K.U., Becker, S., Griesinger, C.: A Combination of spin diffusion methods for the determination of protein-ligand complex structural ensembles. Angew. Chem. Int. Ed. 2015, 54, 6511-6515.

42. Carneiro, M.G., Koharudin, L.M.I., Ban, D., Sabo, T.M., Trigo-Mourino P., Mazur, A., Griesinger, C., Gronenborn, A.M., Lee, D.: Sampling of glycan-bound conformers by the anti-HIV lectin Oscillatoria agardhii agglutinin in the absence of sugar. Angew. Chem. Int. Ed. 2015, 54, 6462-6465.

41. Carneiro, M.G., Koharudin, L.M.I., Griesinger, C., Gronenborn, A.M., Lee, D.: 1H, 13C and 15N resonance assignment of the anti-HIV lectin from Oscillatoria agardhii. Biomol. NMR Assign. 2015, 9, 317-319.

40. Kim, D.H., Lee, C., Cho, Y.J., Lee, S.H., Cha, E.J., Lim, J.E., Sabo, T.M., Griesinger, C., Lee, D., Han, K.H.: A pre-structured helix in the intrinsically disordered 4EBP1. Mol. Biosyst. 2015, 11, 366-369.

39. Smith, C.A., Ban, D., Pratihar, S., Giller, K., Schwiegk, C., de Groot, B.L., Becker, S., Griesinger, C., Lee, D.: Population shuffling of protein conformations. Angew. Chem. Int. Ed. 2015, 54, 207-210.


38. Michielssens, S., Peters, J.H., Ban, D., Pratihar, S., Seeliger, D., Sharma, M., Giller, K., Sabo, T.M., Becker, S., Lee, D., Griesinger, C., de Groot, B.L.: A designed conformational shift to control protein binding specificity. Angew. Chem. Int. Ed. 2014, 53, 10367-10371.

37. Edwards, L.J., Savostyanov, D.V., Welderufael, Z.T., Lee, D., Kuprov, I.: Quantum mechanical NMR simulation algorithm for protein-size spin systems. J. Magn. Reson. 2014, 243, 107-113.

36. Bibow, S., Carneiro, M.G., Sabo, T.M., Schwiegk, C., Becker, S., Riek, R., Lee, D.: Measuring membrane protein bond orientations in nanodics via residual dipolar couplings. Protein Sci. 2014, 23, 851-856.

35. Sabo, T.M., Smith, C.A., Ban, D., Mazur, A., Lee, D., Griesinger, C.: ORIUM: Optimized RDC-based iterative and unified model-free analysis. J. Biomol. NMR 2014, 58, 287-301.

33. Ban, D., Mazur, A., Carneiro, M.G., Sabo, T.M., Giller, K., Koharudin, L.M.I., Becker, S., Gronenborn, A.M., Griesinger, C., Lee, D., Enhanced accuracy of kinetic information from CT-CPMG experiments by transverse rotating-frame spectroscopy. J. Biomol. NMR 2013, 57, 73-82.

32. Mazur, A., Hammesfahr, B., Griesinger, C., Lee, D., Kollmar, M., ShereKhan - Calculating exchange parameters in relaxation dispersion data from CPMG experiments. Bioinformatics 2013, 29, 1819-1820.

31. Himmel, S., Zschiedrich, C., Becker, S., Hsiao, H.-H., Wolff, S., Diethmaier, C., Urlaub, H., Lee, D., Griesinger, C., Stülke, J., Determinants of interaction specificity of the Bacillus subtilis GlcT antitermination protein: Functionality and phosphorylation specificity depend on the arrangement of the regulatory domains. J. Biol. Chem. 2012, 287, 27731-27742.

30. Ban, D., Gossert, A.D., Giller, K., Becker, S., Griesinger, C., Lee, D., Exceeding the limit of dynamics studies on biomolecules using high spin-lock field strengths with a cryogenically cooled probehead. J. Magn. Reson. 2012, 221, 1-4.

29. Meirovitch, E., Lee, D., Walter, K.F.A., Griesinger, C., Standard tensorial analysis of local ordering in proteins from residual dipolar couplings. J. Phys. Chem. B. 2012, 116, 6106-6117.

28. Lee, Y., Zeng, H., Mazur, A., Wegstroth, M., Carlomagno, T., Reese, M., Lee, D., Becker, S., Griesinger C., Hilty, C., Hyperpolarized binding Pocket NOE for determination of competitive ligand binding. Angew. Chem. Int. Ed.2012, 51, 5179-5182.

27. Sabo, T.M., Bakhtiari, D., Walter, K.F.A., McFeeters, R.L., Giller, K., Becker, S., Griesinger, C., Lee, D., Thermal coefficients of the methyl groups within ubiquitin. Protein Sci. 2012, 21, 562-570.

26. 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., Becker, S., Lakomek, N.-A., Lee, D., Lunkenheimer, P., Griesinger, C., Kinetics of conformational sampling in ubiquitin. Angew. Chem. Int. Ed. 2011, 50, 11437-11440.

25. Fenwick, R.B., Esteban-Martin, S., Richter, B., Lee, D., Walter, K.F.A, Milovanovic, 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, 10336-10339.

24. Michel, E., Damberger, F.F., Ishida, Y., Fiorito, F., Lee, D., Leal, W.S., Wüthrich, K., Dynamic conformational equilibria in the physiological function of the Bombyx mori pheromone-binding protein. J. Mol. Biol. 2011, 408, 922-931.


23. Himmel, S., Wolff, S., Becker, S., Lee, D., Griesinger, C., Detection and identification of protein-phosphorylation sites in histidines through HNP correlation patterns. Angew. Chem. Int. Ed. 2010, 49, 8971-8974.

22. Dervillez, X., Klaukien, V., Dürr, R., Koch, J., Kreutz, A., Haarmann, T., Stoll, M., Lee, D., Carlomagno, T., Schnierle, B., Königs, C., Griesinger, C., Dietrich, U., Peptide ligands targeting CD4-induced epitopes on native HIV-1 gp120 mimic CCR5 domains and inhibit HIV-1 entry. J. Virol. 2010, 84, 10131-10138.

21. Rodriguez-Castaneda, F., Maestre-Martinez, M., Coudevylle, N., Dimova, K., Junge, H., Lipstein, N., Lee, D., Becker, S., Brose, N., Jahn, O., Carlomagno, T., Griesinger, C., Modular architecture of the Munc13-1/calmodulin complex enables short-term plasticity. EMBO J. 2010, 29, 680-691.

20. Lee, D., Vijayan, V., Montaville, P., Becker, S., Griesinger, C., Sensitivity enhancement of methyl-TROSY by longitudinal 1H relaxation optimization. J. Kor. Magn. Reson. Soc. 2009, 13, 15-26.

19. Schmidt, H., Himmel, S., Walter, K.F.A., Klaukien, V., Funk, M., Lee, D., Transverse relaxation-optimized HCN experiment for tautomeric states of histidine sidechains. J. Kor. Magn. Reson. Soc. 2008, 12, 89-95.

18. Lee, D., Walter, K.F.A., Brückner, A.-K., Hilty, C., Becker, S., Griesinger, C., Bilayer in small bicelles revealed by lipid-protein interactions using NMR spectroscopy. J. Am. Chem. Soc. 2008, 130, 13822-13823.

17. Lee, D., Walsh, J.D., Migliorini, M., Yu, P., Cai, T., Schwieters, C.D., Krueger, S., Strickland, D.K., Wang, Y.-X., The structure of receptor-associated protein (RAP). Protein Sci. 2007, 16, 1628-1640.

16. Bae, E., Reiter, N.J, Bingman, C.A., Kwan, S., Lee, D., Philips, G.N. Jr., Butcher, S.E., Brow, D.A., Structure and interactions of the first three RNA recognition motifs of splicing factor Prp24. J. Mol. Biol. 2007, 367, 1447-1458.

15. Lee, D., Walsh, J.D., Yu, P., Markus, M.A., Choli-Papadopoulou, T., Schwieters, C.D., Krueger, S., Draper, D.E., Wang, Y.-X., The structure of free L11 and functional dynamic of L11 in free, L11-rRNA(58nt) binary and L11-rRNA(58nt)-thiostrepton ternary complexes. J. Mol. Biol. 2007, 367, 1007-1022.

14. Reiter, N.J, Lee, D., Wang, Y.-X., Tonelli, M., Bahrami, A., Cornilescu, C.C., Butcher, S.E., Resonance assignments for the two N-terminal RNA recognition motifs (RRM) of the S. cerevisiae Pre-mRNA Processing Protein Prp24. J. Biomol. NMR 2006, 36, S5, 58.

13. Lee, D., Walsh, J.D., Migliorini, M., Yu, P., Strickland, D.K., Wang, Y.-X., NMR assignments of domain 3 of receptor-associated protein (RAP). J. Biomol. NMR 2006, 36, S5, 56.

12. Walsh, J.D., Lee, D., Migliorini, M., Yu, P., Strickland, D.K., Wang, Y.-X., NMR assignment of domain 2 of receptor-associated protein. J. Biomol. NMR 2006, 36, S5, 54.

11. Lee, D., Walsh, J.D., Mikhailenko, I., Yu, P., Migliorini, M., Wu, Y., Krueger, S., Curtis, J.E., Harris, B., Lockett, S., Blacklow, S.C., Strickland, D.K., Wang, Y.-X., RAP uses a histidine switch to regulate its interaction with LRP in the ER and Golgi. Mol. Cell 2006, 22, 423-430.

10. Lee, D., Hilty, C., Wider, G., Wüthrich, K., Effective rotational correlation times of proteins from NMR relaxation interference. J. Magn. Reson. 2006, 178, 72-76.

9. Lee, D., Pervushin, K., Bischof, D., Braun, M., Thöny-Meyer, L., Unusual heme-histidine bond in the active site of a chaperone. J. Am. Chem. Soc. 2005, 127, 3716-3717.

8. Lee, D., Vögeli, B., Pervushin K., Detection of C’,Cα correlations in proteins using a new time- and sensitivity-optimal experiment. J. Biomol. NMR 2005, 31, 273-278.

7. Bromek, K., Lee, D., Hauhart, R., Krych-Goldberg, M., Atkinson, J.P., Barlow, P.N., Pervushin, K., Polychromatic selective population inversion for TROSY experiments with large proteins. J. Am. Chem. Soc. 2005, 127, 405-411.

6. Lee, D., Damberger, F.F., Peng, G., Horst, R., Güntert, P., Nikonova, L., Leal, W.S., Wüthrich, K., NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH. FEBS Lett. 2002, 531, 314-318.

5. Shin, J., Lee, W., Lee, D., Koo, B.-K., Lim, Y., Woods, A., Couchman, J.R., Oh, E.-S., Solution structure of the dimeric cytoplasmic domain of syndecan-4. Biochemistry 2001, 40, 8471-8478.

4. Cho, H.-S., Ha, N.-C., Choi, G., Kim, H.-J., Lee, D., Oh, K.S., Kim, K.S., Lee, W., Choi, K.W., Oh, B.-H., Crystal structure of Δ5-3-ketosteroid isomerase from Pseudomonas testosteroni in complex with equilenin settles the correct hydrogen bonding scheme for transition state stabilization. J. Biol. Chem. 1999, 274, 32863-32868.

1. Lee, D., Oh, E.-S., Woods, A., Couchman, J.R., Lee, W., Solution structure of a syndecan-4 cytoplasmic domain and its interaction with phosphatidylinositol 4,5-bisphosphate. J. Biol. Chem. 1998, 273, 13022-13029.