1. NMR Assignment of HI1506, a Novel Two-domain Protein from Haemophilus influenzae.
N. Sari, D. C. Yeh, V. Doseeva, K. Surabian, O. Herzberg and J. Orban; Journal of Biomolecular NMR, 2005; 33(4) 281-282
2. Solution NMR structures of IgG-binding Domains with artificially evolved high sequence identity but different folds
Y. He, D.C. Yeh, P. Alexander, P. Bryan, J. Orban; Biochemistry, 2005; 44, 14055-14061
3. Solution NMR structure of the hypothetical protein HI0004 from Haemophilus Influenzae, and comparison with the X-ray structure of an Aquifex aeolicus homolog
D.C. Yeh, L. Parsons, M. Eisenstein, J. Orban; Protein Science, 2005; 14, 424-430
4. Integrating structural genomics and functional genomics
L. Parsons, F. Liu, D.C. Yeh, N. Sari, J. Orban;
Austalian Journal of Chemistry, 2004; 57(7), 619-623
5. Solution NMR structure of the highly acidic protein HI1450 from Haemophilus Influenzae - a putative double stranded DNA mimic.
L. Parsons, D.C. Yeh, J. Orban; Proteins: Structure, Function and Bioinformatics, 2004; 54, 375-383
6. NMR assignment of the hypothetical protein HI1723 from Haemophilus Influenzae - sequence homologue from the iron sulfur cluster assembly (Isc A) family.
D.C. Yeh, F. Liu, N. Bonander, E. Eisenstein, J. Orban; Journal of Biomolecular NMR, 2004; 29(2), 213-214
7. NMR assignment of the hypothetical protein HI0004 from Haemophilus Influenzae - a putative essential gene product.
D.C. Yeh, J. Parsons, L. Parsons, F. Liu, E. Eisenstein, J. Orban; Journal of Biomolecular NMR, 2004; 29(1), 101-102
8. Assisting functional assignment for hypothetical Haemophilus Influenzae gene products through structural genomics.
G. L. Gilland, A. Teplyakov, G. Obmolova, M. Tordova, N. Thanki, J. Ladner, O. Herzberg, K. Lim, H. Zhang, K. Huang, Z. Li, A. Tempczyk, W. Krajewski, L. Parsons, D.C. Yeh, J. Orban, A. J. Howard, E. Eisenstein, J. F. Parsons, N. Bonander, K. E. Fisher, J. Toedt, P. Reddy, C.V. Rao, E. Melamud and J. Moult; Current Drug Targets-Infectious Disorders, 2002; 2, 339-353
9. Reduced dimensionality NMR spectroscopy for high-throughput protein resonance assignment.
T. Szyperski, D.C. Yeh, H. Moseley, G. Montelione; Proceedings of the National Academy of the Science of USA, 2002; 99, 8009-8014
10. Solution 1H NMR of the active site of substrate-bound, cyanide-inhibited human heme oxygenase: Comparison to the crystal structure of the water-ligated form.
G.N. La Mar A. Asokan, B. Espiritu, D.C. Yeh, K. Auclair, P.R. O. Montellano; Journal of Biological Chemistry, 2001; 276(19), 15676-15687.
11. Solution 1H NMR study of the heme cavity and folding topology of the abbreviated Chain 118-residue globin from the cyanobacterium Nostoc Commune.
D.C. Yeh, M. V. Thorsteinson, D. R. Bevan, M. Plotts, and G. N. La Mar; Biochemistry, 2000; 39(6), 1389-1399.
12. Solution NMR determination of the anisotropy and orientation of the paramagnetic susceptibility tensor as a function of temperature for myoglobin cyanide: Implication for the population of the excited electronic state.
B. D. Nguyen, Z. Xia, D.C. Yeh, K. Vyas, H. Deaguero, G. N. La Mar; Journal of the American Chemical Society, 1999; 121(1), 208-217.
13. Solution 1H NMR investigation of the molecular and electronic structure of the active site of the substrate-bound heme oxygenase: the nature of distal H-bond donor to bound ligands.
C.M. Gorst, A. Wilks, D.C. Yeh, C. Montellano, G. N. La Mar
; Journal of the American Chemical Society, 1998; 120(34), 8875-8884.
14. In vivo NMR spectroscopy of high -energy phosphorous metabolism in the forearm muscle: Comparison between elite athletes and sedentaries. T.H. Lim, M. Jin Shin, D. C.Yeh, T.K. Lee, Y.Yi, Y.S. Jin, D. S. Chung; Korean Journal of Radiology, 1991; 27(6), 873-880.
15. HPLC determination of carboxyl group using 2-bromoacetyl triphenylene as pre-labeling reagent(III): Separative determination of glycyrrhetinic acid contained in licorice powder.
H.S. Jung, D.C.Yeh, B.K. Kim, M. K. Park, W.K. Lee; Yakhak Hoeji,1987; 31(5), 315-
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