Publications

Publication List

[77] D. Szöllősi, S. Pratihar, D. Mukhopadhyay, A. K. Rout, G. J. Reddy, et al. "Hierarchically ordered multi-timescale structural dynamics of the intrinsically disordered p53 transactivation domain." bioRxiv, 2025.08.01.668138 (2025). DOI: https://doi.org/10.1101/2025.08.01.668138

[76] K. Han, E. Kim, K. S. Ryu, and D. Lee. "A robust, deep learning-based analysis of time-domain signals for NMR spectroscopy." Journal of Analytical Science and Technology 16 (1), 3 (2025). DOI: https://doi.org/10.1186/s40543-024-00414-z

[75] H. M. Jung, J. H. Ha, M. V. C. dela Cerna, J. A. Burlison, J. Choi, B. R. Kim, J. K. Bang, et al. "An innovative inhibitor with a new chemical moiety aimed at biliverdin IX$\beta$ reductase for thrombocytopenia and resilient against cellular degradation." Pharmaceutics 16 (9), 1148 (2024). DOI: https://doi.org/10.3390/pharmaceutics16091148

[74] D. H. Seo, Y. H. Huh, H. K. Cheong, E. H. Kim, J. S. Lim, M. J. Lee, D. Lee, and K. S. Ryu. "Mechanism of methylene blue inducing the disulfide bond formation of tubulin-associated unit proteins." JACS Au 4 (7), 2451-2455 (2024). DOI: https://doi.org/10.1021/jacsau.4c00298

[73] J. Choi, S. Tak, H. M. Jung, S. Cha, E. Hwang, D. Lee, J. H. Lee, K. S. Ryu, and C. Park. "Kinetic evidence in favor of glyoxalase III and against deglycase activity of DJ-1." Protein Science 32 (5), e4641 (2023). DOI: https://doi.org/10.1002/pro.4641

[72] K. S. Chakrabarti, S. Olsson, S. Pratihar, K. Giller, K. Overkamp, K. O. Lee, et al. "A litmus test for classifying recognition mechanisms of transiently binding proteins." Nature Communications 13 (1), 3792 (2022). DOI: https://doi.org/10.1038/s41467-022-31374-5

[71] K. S. Chakrabarti, S. Pratihar, K. Giller, K. Overkamp, K. O. Lee, K. S. Ryu, et al. "High-power relaxation dispersion NMR data set at different ligand concentrations: a litmus test for classification of recognition mechanism." Edmond, MPDL (2022). DOI: https://doi.org/10.17617/3.88

[70] M. Kim, J. H. Ha, J. Choi, B. R. Kim, V. Gapsys, K. O. Lee, J. G. Jee, K. S. Chakrabarti, et al. "Repositioning Food and Drug Administration-approved drugs for inhibiting biliverdin IX$\beta$ reductase B as a novel thrombocytopenia therapeutic target." Journal of Medicinal Chemistry 65 (3), 2548-2557 (2022). DOI: https://doi.org/10.1021/acs.jmedchem.1c01828

[69] D. R. Rivas, M. V. C. Dela Cerna, C. N. Smith, S. Sampathi, B. G. Patty, D. Lee, et al. "A screen of FDA-approved drugs identifies inhibitors of protein tyrosine phosphatase 4A3 (PTP4A3 or PRL-3)." Scientific Reports 11 (1), 10302 (2021). DOI: https://doi.org/10.1038/s41598-021-89721-5

[68] J. Lee, Z. Jin, D. Lee, J. H. Yun, and W. Lee. "Characteristic analysis of homo- and heterodimeric complexes of human mitochondrial pyruvate carrier related to metabolic diseases." International Journal of Molecular Sciences 21 (9), 3403 (2020). DOI: https://doi.org/10.3390/ijms21093403

[67] S. C. Elmoustapha, M. V. C. Dela Cerna, and D. Lee. "Identification of small molecules targeting the MdmX-p53 interaction in human cancers." Methods in Molecular Biology 2098, 119-131 (2020). DOI: https://doi.org/10.1007/978-1-62703-236-0_8

[66] C. A. Smith, A. Mazur, A. K. Rout, S. Becker, D. Lee, B. L. De Groot, and C. Griesinger. "Enhancing NMR derived ensembles with kinetics on multiple timescales." Journal of Biomolecular NMR 74 (1), 27-43 (2020). DOI: https://doi.org/10.1007/s10858-019-00289-4

[65] N. Khan, J. Park, W. L. Dean, R. D. Gray, W. Tse, D. Lee, and T. M. Sabo. "Recombinant expression and purification of AF1q and its interaction with T-cell factor 7." Protein Expression and Purification 165, 105499 (2020). DOI: https://doi.org/10.1016/j.pep.2019.105499

[64] N. Khan, P. P. Shah, D. Ban, P. Trigo-Mourino, M. G. Carneiro, L. DeLeeuw, et al. "Solution structure and functional investigation of human guanylate kinase reveals allosteric networking." Journal of Biological Chemistry 294 (31), 11920-11933 (2020). DOI: https://doi.org/10.1074/jbc.RA119.008688

[63] K. M. Tyo, J. Duan, P. Kollipara, M. V. C. dela Cerna, D. Lee, K. E. Palmer, et al. "pH-responsive delivery of griffithsin from electrospun fibers." European Journal of Pharmaceutics and Biopharmaceutics 138, 64-74 (2019). DOI: https://doi.org/10.1016/j.ejpb.2019.03.013

[62] T. M. Sabo and D. Lee. "New methods in biomolecular nuclear magnetic resonance spectroscopy." Methods 138, 1-2 (2018). DOI: https://doi.org/10.1016/j.ymeth.2018.04.019

[61] T. M. Sabo, V. Gapsys, K. F. A. Walter, R. B. Fenwick, S. Becker, X. Salvatella, et al. "Utilizing dipole-dipole cross-correlated relaxation for the measurement of angles between pairs of opposing C$\alpha$H$\alpha$-C$\alpha$H$\alpha$ bonds in anti-parallel $\beta$-sheets." Methods 138, 85-92 (2018). DOI: https://doi.org/10.1016/j.ymeth.2018.01.006

[60] N. Khan, D. Ban, P. Trigo-Mourino, M. G. Carneiro, M. Konrad, D. Lee, et al. "$^1$H, $^{13}$C and $^{15}$N resonance assignment of human guanylate kinase." Biomolecular NMR Assignments 12 (1), 11-14 (2018). DOI: https://doi.org/10.1007/s12104-017-9774-3

[59] T. Ikeya, D. Ban, D. Lee, Y. Ito, K. Kato, and C. Griesinger. "Solution NMR views of dynamical ordering of biomacromolecules." Biochimica et Biophysica Acta (BBA)-General Subjects 1862 (2), 287-306 (2018). DOI: https://doi.org/10.1016/j.bbagen.2017.10.015

[58] T. M. Sabo and D. Lee. "NMR methods of characterizing biomolecular structural dynamics and conformational ensembles." Methods 148, 1-3 (2018). DOI: https://doi.org/10.1016/j.ymeth.2018.05.004

[57] J. G. Reddy, S. Pratihar, D. Ban, S. Frischkorn, S. Becker, C. Griesinger, and D. Lee. "Simultaneous determination of fast and slow dynamics in molecules using extreme CPMG relaxation dispersion experiments." Journal of Biomolecular NMR 70 (1), 1-9 (2018). DOI: https://doi.org/10.1007/s10858-017-0153-6

[56] P. Trigo-Mouriño, C. Griesinger, and D. Lee. "Label-free NMR-based dissociation kinetics determination." Journal of Biomolecular NMR 69 (4), 229-235 (2017). DOI: https://doi.org/10.1007/s10858-017-0145-6

[55] D. Ban, C. A. Smith, B. L. de Groot, C. Griesinger, and D. Lee. "Recent advances in measuring the kinetics of biomolecules by NMR relaxation dispersion spectroscopy." Archives of Biochemistry and Biophysics 628, 81-91 (2017). DOI: https://doi.org/10.1016/j.abb.2017.06.014

[54] S. Pratihar, T. M. Sabo, D. Ban, R. B. Fenwick, S. Becker, X. Salvatella, et al. "Kinetics of the antibody recognition site in the third IgG-binding domain of protein G." Angewandte Chemie International Edition 55 (33), 9567-9570 (2016). DOI: https://doi.org/10.1002/anie.201603525

[53] K. S. Chakrabarti, D. Ban, S. Pratihar, J. G. Reddy, S. Becker, C. Griesinger, et al. "High-power $^1$H composite pulse decoupling provides artifact free exchange-mediated saturation transfer (EST) experiments." Journal of Magnetic Resonance 269, 65-69 (2016). DOI: https://doi.org/10.1016/j.jmr.2016.05.011

[52] C. A. Smith, D. Ban, S. Pratihar, K. Giller, M. Paulat, S. Becker, C. Griesinger, et al. "Allosteric switch regulates protein-protein binding through collective motion." Proceedings of the National Academy of Sciences 113 (12), 3269-3274 (2016). DOI: https://doi.org/10.1073/pnas.1521743113

[51] C. A. Smith, A. Mazur, D. Ban, S. Becker, C. Griesinger, D. Lee, and B. L. de Groot. "Allostery through protein motion at different length and time scales." Biophysical Journal 110 (3), 221a (2016). DOI: https://doi.org/10.1016/j.bpj.2015.11.1219

[50] T. M. Sabo, J. O. Trent, and D. Lee. "Population shuffling between ground and high energy excited states." Protein Science 24 (11), 1714-1719 (2015). DOI: https://doi.org/10.1002/pro.2755

[49] M. G. Carneiro, J. G. Reddy, C. Griesinger, and D. Lee. "Speeding-up exchange-mediated saturation transfer experiments by Fourier transform." Journal of Biomolecular NMR 63 (3), 237-244 (2015). DOI: https://doi.org/10.1007/s10858-015-9983-z

[48] M. G. Carneiro, L. M. I. Koharudin, C. Griesinger, A. M. Gronenborn, and D. Lee. "$^1$H, $^{13}$C and $^{15}$N resonance assignment of the anti-HIV lectin from Oscillatoria agardhii." Biomolecular NMR Assignments 9 (2), 317-319 (2015). DOI: https://doi.org/10.1007/s12104-015-9598-y

[47] J. Pilger, A. Mazur, P. Monecke, H. Schreuder, B. Elshorst, S. Bartoschek, et al. "A combination of spin diffusion methods for the determination of protein-ligand complex structural ensembles." Angewandte Chemie 127 (22), 6611-6615 (2015). DOI: https://doi.org/10.1002/ange.201501416

[46] M. G. Carneiro, L. M. I. Koharudin, D. Ban, T. M. Sabo, P. Trigo-Mourino, A. Mazur, et al. "Sampling of glycan-bound conformers by the anti-HIV lectin OAA in the absence of sugar." Angewandte Chemie 127 (22), 6562-6565 (2015). DOI: https://doi.org/10.1002/ange.201500318

[45] D. H. Kim, C. Lee, Y. J. Cho, S. H. Lee, E. J. Cha, J. E. Lim, T. M. Sabo, C. Griesinger, et al. "A pre-structured helix in the intrinsically disordered 4EBP1." Molecular BioSystems 11 (2), 366-369 (2015). DOI: https://doi.org/10.1039/C4MB00627G

[44] C. A. Smith, D. Ban, K. Giller, S. Becker, C. Griesinger, D. Lee, and B. L. de Groot. "Microsecond motion modulates ubiquitin binding through an allosteric backbone/side chain network." Biophysical Journal 108 (2), 184a-185a (2015). DOI: https://doi.org/10.1016/j.bpj.2014.11.1015

[43] C. A. Smith, D. Ban, S. Pratihar, K. Giller, C. Schwiegk, B. L. de Groot, S. Becker, et al. "Population shuffling of protein conformations." Angewandte Chemie International Edition 54 (1), 207-210 (2015). DOI: https://doi.org/10.1002/anie.201407335

[42] S. Michielssens, J. H. Peters, D. Ban, S. Pratihar, D. Seeliger, M. Sharma, et al. "A designed conformational shift to control protein binding specificity." Angewandte Chemie International Edition 53 (39), 10367-10371 (2014). DOI: https://doi.org/10.1002/anie.201404628

[41] S. Bibow, M. G. Carneiro, T. M. Sabo, C. Schwiegk, S. Becker, R. Riek, and D. Lee. "Measuring membrane protein bond orientations in nanodiscs via residual dipolar couplings." Protein Science 23 (7), 851-856 (2014). DOI: https://doi.org/10.1002/pro.2468

[40] T. M. Sabo, C. A. Smith, D. Ban, A. Mazur, D. Lee, and C. Griesinger. "ORIUM: Optimized RDC-based iterative and unified model-free analysis." Journal of Biomolecular NMR 58 (4), 287-301 (2014). DOI: https://doi.org/10.1007/s10858-014-9824-5

[39] D. Ban, T. M. Sabo, C. Griesinger, and D. Lee. "Measuring dynamic and kinetic information in the previously inaccessible supra-$\tau_c$ window by solution NMR spectroscopy." Molecules 18 (10), 11904-11937 (2013). DOI: https://doi.org/10.3390/molecules181011904

[38] D. Ban, A. Mazur, M. G. Carneiro, T. M. Sabo, K. Giller, L. M. I. Koharudin, et al. "Enhanced accuracy of kinetic information from CT-CPMG experiments by transverse rotating-frame spectroscopy." Journal of Biomolecular NMR 57 (1), 73-82 (2013). DOI: https://doi.org/10.1007/s10858-013-9762-7

[37] A. Mazur, B. Hammesfahr, C. Griesinger, D. Lee, and M. Kollmar. "ShereKhan: Calculating exchange parameters in relaxation dispersion data from CPMG experiments." Bioinformatics 29 (14), 1819-1820 (2013). DOI: https://doi.org/10.1093/bioinformatics/btt289

[36] C. A. Smith, D. Ban, J. H. Peters, K. Giller, S. Becker, B. L. de Groot, C. Griesinger, et al. "Molecular recognition through concerted ubiquitin backbone and side chain motion." Biophysical Journal 104 (2), 30a (2013). DOI: https://doi.org/10.1016/j.bpj.2012.11.203

[35] S. Himmel, C. P. Zschiedrich, S. Becker, H. H. Hsiao, S. Wolff, C. Diethmaier, et al. "Determinants of interaction specificity of the Bacillus subtilis GlcT antitermination protein." Journal of Biological Chemistry 287 (33), 27731-27742 (2012). DOI: https://doi.org/10.1074/jbc.M112.359646

[34] D. Ban, A. D. Gossert, K. Giller, S. Becker, C. Griesinger, and D. Lee. "Exceeding the limit of dynamics studies on biomolecules using high spin-lock field strengths." Journal of Magnetic Resonance 221, 1-4 (2012). DOI: https://doi.org/10.1016/j.jmr.2012.05.011

[33] E. Meirovitch, D. Lee, K. F. A. Walter, and C. Griesinger. "Standard tensorial analysis of local ordering in proteins from residual dipolar couplings." The Journal of Physical Chemistry B 116 (21), 6106-6117 (2012). DOI: https://doi.org/10.1021/jp301825j

[32] Y. Lee, H. Zeng, A. Mazur, M. Wegstroth, T. Carlomagno, M. Reese, D. Lee, et al. "Hyperpolarized binding pocket nuclear Overhauser effect for determination of competitive ligand binding." Angewandte Chemie 124 (21), 5269-5272 (2012). DOI: https://doi.org/10.1002/ange.201201416

[31] T. M. Sabo, D. Bakhtiari, K. F. A. Walter, R. L. McFeeters, K. Giller, S. Becker, et al. "Thermal coefficients of the methyl groups within ubiquitin." Protein Science 21 (4), 562-570 (2012). DOI: https://doi.org/10.1002/pro.2041

[30] D. Ban, M. Funk, R. Gulich, D. Egger, T. M. Sabo, K. F. A. Walter, R. B. Fenwick, et al. "Kinetics of conformational sampling in ubiquitin." Angewandte Chemie 123 (48), 11639-11642 (2011). DOI: https://doi.org/10.1002/ange.201104996

[29] R. B. Fenwick, S. Esteban-Martín, B. Richter, D. Lee, K. F. A. Walter, et al. "Weak long-range correlated motions in a surface patch of ubiquitin involved in molecular recognition." Journal of the American Chemical Society 133 (27), 10336-10339 (2011). DOI: https://doi.org/10.1021/ja202867v

[28] E. Michel, F. F. Damberger, Y. Ishida, F. Fiorito, D. Lee, W. S. Leal, and K. Wüthrich. "Dynamic conformational equilibria in the physiological function of the Bombyx mori pheromone-binding protein." Journal of Molecular Biology 408 (5), 922-931 (2011). DOI: https://doi.org/10.1016/j.jmb.2011.03.012

[27] S. Himmel, S. Wolff, S. Becker, D. Lee, and C. Griesinger. "Detection and identification of protein-phosphorylation sites in histidines through HNP correlation patterns." Angewandte Chemie International Edition 49 (47), 8971-8974 (2010). DOI: https://doi.org/10.1002/anie.201004112

[26] X. Dervillez, V. Klaukien, R. Dürr, J. Koch, A. Kreutz, T. Haarmann, M. Stoll, et al. "Peptide ligands selected with CD4-induced epitopes on native dualtropic HIV-1 envelope proteins mimic extracellular coreceptor domains." Journal of Virology 84 (19), 10131-10138 (2010). DOI: https://doi.org/10.1128/JVI.00844-10

[25] F. Rodríguez-Castañeda, M. Maestre-Martínez, N. Coudevylle, K. Dimova, et al. "Modular architecture of Munc13/calmodulin complexes." The EMBO Journal 29 (3), 680-691 (2010). DOI: https://doi.org/10.1038/emboj.2009.373

[24] D. H. Lee, V. Vijayan, P. Montaville, S. Becker, and C. Griesinger. "Sensitivity enhancement of Methyl-TROSY by longitudinal $^1$H relaxation optimization." Journal of the Korean Magnetic Resonance Society 13 (1), 15-26 (2009). DOI: https://doi.org/10.6564/JKMRS.2009.13.1.015

[23] D. Lee, K. F. A. Walter, A. K. Brückner, C. Hilty, S. Becker, and C. Griesinger. "Bilayer in small bicelles revealed by lipid-protein interactions using NMR spectroscopy." Journal of the American Chemical Society 130 (42), 13822-13823 (2008). DOI: https://doi.org/10.1021/ja804961m

[22] H. Schmidt, S. Himmel, K. F. A. Walter, V. Klaukien, M. Funk, and D. H. Lee. "Transverse relaxation-optimized HCN experiment for tautomeric states of histidine sidechains." Journal of the Korean Magnetic Resonance Society 12 (2), 89-95 (2008). DOI: https://doi.org/10.6564/JKMRS.2008.12.2.089

[21] D. Lee, J. D. Walsh, M. Migliorini, P. Yu, T. Cai, C. D. Schwieters, S. Krueger, et al. "The structure of receptor-associated protein (RAP)." Protein Science 16 (8), 1628-1640 (2007). DOI: https://doi.org/10.1110/ps.072895107

[20] E. Bae, N. J. Reiter, C. A. Bingman, S. S. Kwan, D. Lee, G. N. Phillips Jr, et al. "Structure and interactions of the first three RNA recognition motifs of splicing factor Prp24." Journal of Molecular Biology 367 (5), 1447-1458 (2007). DOI: https://doi.org/10.1016/j.jmb.2007.01.066

[19] D. Lee, J. D. Walsh, P. Yu, M. A. Markus, T. Choli-Papadopoulou, et al. "The structure of free L11 and functional dynamics of L11 in free and ternary complexes." Journal of Molecular Biology 367 (4), 1007-1022 (2007). DOI: https://doi.org/10.1016/j.jmb.2007.01.045

[18] J. D. Walsh, D. Lee, P. Yu, M. Migliorini, D. K. Strickland, and Y. X. Wang. "NMR assignment of domain 2 of the receptor-associated protein." Journal of Biomolecular NMR 36 (Suppl 1), 54-54 (2006). DOI: https://doi.org/10.1007/s10858-006-9008-8

[17] D. Lee, J. D. Walsh, P. Yu, M. Migliorini, Y. Wu, D. K. Strickland, and Y. X. Wang. "NMR assignment of domain 3 of the receptor-associated protein (RAP)." Journal of Biomolecular NMR 36 (Suppl 1), 56-56 (2006). DOI: https://doi.org/10.1007/s10858-006-9010-1

[16] N. J. Reiter, D. Lee, Y. X. Wang, M. Tonelli, A. Bahrami, C. C. Cornilescu, et al. "Resonance assignments for the two N-terminal RNA recognition motifs of Prp24." Journal of Biomolecular NMR 36 (Suppl 1), 58-58 (2006). DOI: https://doi.org/10.1007/s10858-006-9011-0

[15] D. Lee, J. D. Walsh, I. Mikhailenko, P. Yu, M. Migliorini, Y. Wu, S. Krueger, et al. "RAP uses a histidine switch to regulate its interaction with LRP in the ER and Golgi." Molecular Cell 22 (3), 423-430 (2006). DOI: https://doi.org/10.1016/j.molcel.2006.03.024

[14] D. Lee, C. Hilty, G. Wider, and K. Wüthrich. "Effective rotational correlation times of proteins from NMR relaxation interference." Journal of Magnetic Resonance 178 (1), 72-76 (2006). DOI: https://doi.org/10.1016/j.jmr.2005.08.012

[13] D. Lee, B. Vögeli, and K. Pervushin. "Detection of C', C$\alpha$ correlations in proteins using a new time- and sensitivity-optimal experiment." Journal of Biomolecular NMR 31 (4), 273-278 (2005). DOI: https://doi.org/10.1007/s10858-005-2426-3

[12] D. Lee, K. Pervushin, D. Bischof, M. Braun, and L. Thöny-Meyer. "Unusual heme-histidine bond in the active site of a chaperone." Journal of the American Chemical Society 127 (11), 3716-3717 (2005). DOI: https://doi.org/10.1021/ja042571x

[11] K. Bromek, D. Lee, R. Hauhart, M. Krych-Goldberg, J. P. Atkinson, P. N. Barlow, et al. "Polychromatic selective population inversion for TROSY experiments with large proteins." Journal of the American Chemical Society 127 (1), 405-411 (2005). DOI: https://doi.org/10.1021/ja045233a

[10] D. Lee, F. F. Damberger, G. Peng, R. Horst, P. Güntert, L. Nikonova, W. S. Leal, et al. "NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH." FEBS Letters 531 (2), 314-318 (2002). DOI: https://doi.org/10.1016/S0014-5793(02)03541-6

[9] J. Shin, W. Lee, D. Lee, B. K. Koo, I. Han, Y. Lim, A. Woods, J. R. Couchman, et al. "Solution structure of the dimeric cytoplasmic domain of syndecan-4." Biochemistry 40 (29), 8471-8478 (2001). DOI: https://doi.org/10.1021/bi0027731

[8] H. S. Cho, N. C. Ha, G. Choi, H. J. Kim, D. Lee, K. S. Oh, K. S. Kim, W. Lee, K. Y. Choi, et al. "Crystal structure of $\Delta^5$-3-ketosteroid isomerase from Pseudomonas testosteroni in complex with equilenin." Journal of Biological Chemistry 274 (46), 32863-32868 (1999). DOI: https://doi.org/10.1074/jbc.274.46.32863

[7] J. H. Lee, S. K. Lim, S. H. Huh, D. Lee, and W. Lee. "Solution structures of the melanocyte-stimulating hormones by two-dimensional NMR spectroscopy." European Journal of Biochemistry 257 (1), 31-40 (1998). DOI: https://doi.org/10.1046/j.1432-1327.1998.2570031.x

[6] D. Lee, E. S. Oh, A. Woods, J. R. Couchman, and W. Lee. "Solution structure of a syndecan-4 cytoplasmic domain and its interaction with phosphatidylinositol 4, 5-bisphosphate." Journal of Biological Chemistry 273 (21), 13022-13029 (1998). DOI: https://doi.org/10.1074/jbc.273.21.13022

[5] D. Lee and W. Lee. "An influence of the exchange rate on NOE intensities of a ligand: Application to 37kDa trp-holo-repressor/operator DNA complex." Journal of the Korean Magnetic Resonance Society 2 (1), 33-40 (1998). DOI: https://doi.org/10.6564/JKMRS.1998.2.1.033

[4] D. Lee, S. H. Huh, J. H. Lee, S. K. Lim, and W. Lee. "A study on the solution structure of $\alpha$-melanocyte stimulating hormone by NMR spectroscopy." Journal of the Korean Magnetic Resonance Society 1 (1), 45-55 (1997). DOI: https://doi.org/10.6564/JKMRS.1997.1.1.045

[3] D. Lee, K. S. Oh, K. S. Kim, Y. Lim, and W. Lee. "Structural study of horse heart myoglobin by 2D NMR spectroscopy." Journal of the Korean Magnetic Resonance Society 1 (2), 115-124 (1997). DOI: https://doi.org/10.6564/JKMRS.1997.1.2.115

[2] D. Lee, C. H. Kim, and W. Lee. "NMR studies on the hydrogen bonding schemes of $\Delta^5$-3-ketosteroid isomerase." Journal of the Korean Magnetic Resonance Society 1 (1), 33-44 (1997). DOI: https://doi.org/10.6564/JKMRS.1997.1.1.033

[1] D. Lee and W. Lee. "Nuclear magnetic resonance studies of protein-DNA interactions." Bulletin of the Korean Chemical Society 15, 11-20 (1994). DOI: https://doi.org/10.5012/bkcs.1994.15.1.11