IUPUI NMR Center Publications

   1.  K. V. Vasavada, B. D. Ray, and B. D. Nageswara Rao, 31P NMR Lineshapes of γ-P(ATP) in Presence of Mg2+ and Ca2+:  Estimate of Exchange Rates, J. Inorg. Biochem. 21, 323-335 (1984).

   2.  M. D. Kemple, B. D. Ray, G. K. Jarori, B. D. Nageswara Rao, and F. G. Prendergast, Electron Paramagnetic Resonance of Spin Labelled Aequorin, Biochemistry 23, 4383-4390 (1984).

   3.  G. K. Jarori, B. D. Ray, and B. D. Nageswara Rao, Structure of Metal-Nucleotide Complexes Bound to Creatine Kinase: 31P NMR Measurements Using Mn(II) and Co(II), Biochemistry 24, 3487-3494 (1985).

   4.  B. D. Ray, S. Ho, M. D. Kemple, F. G. Prendergast, and B. D. Nageswara Rao, Proton NMR of Aequorin.  Structural Changes Concomitant with Calcium-Independent Light Emission, Biochemistry 24, 4280-4287 (1985).

   5.  B. D. Nageswara Rao, Structure of Enzyme-Bound Substrate Complexes of Some ATP-Utilizing Enzymes, in K.S. Bruzik and W. J. Stec, eds., Biophosphates and Their Analogues – Synthesis, Structure, Metabolism, and Activity, pp. 547-559, Elsevier Science, The Netherlands (1987).

   6.  B. R. Branchini, F. G. Prendergast, G. A. Spencer, J. D. Hugdahl, B. D.Ray, and M. D. Kemple, Synthesis of Racemic [2'-13C]Tryptophan, J. Lab. Comp. & Radiopharm. 24, 637-643 (1987).

   7.  A. J. Weaver, M. D. Kemple, and F. G. Prendergast, Tryptophan Sidechain Dynamics in Hydrophobic Oligopeptides Determined by Use of 13C NMR Spectroscopy, Biophys. J. 54, 1-15 (1988).

   8.  B. D. Ray, and B. D. Nageswara Rao, 31P NMR Studies of Enzyme-Bound Substrate Complexes of 3-Phosphoglycerate Kinase:  I.  Effects of Sulfate and pH; Mg(II) Affinity at the Two ATP Sites, Biochemistry 27, 5574-5578 (1988).

   9.  B. D. Ray, and B. D. Nageswara Rao, 31P NMR Studies of Enzyme-Bound Substrate Complexes of 3-Phosphoglycerate Kinase:  II.  Structure of the Enzyme-Metal-Nucleotide Complexes, Biochemistry 27, 5579-5585 (1988).

10.  B. D. Ray, P. Rosch, and B. D.Nageswara Rao, 31P NMR Studies of the Structure of Cation-Nucleotide Complexes Bound to Porcine Muscle Adenylate Kinase, Biochemistry 27, 8669-8676 (1988).

11.  M. D. Kemple, B. D. Ray, K. B. Lipkowitz, F. G. Prendergast, and B. D. Nageswara Rao, The Use of Lanthanides for Solution Structure Determination of Biomolecules by NMR:   Evaluation of the Methodology with EDTA Derivatives as Model Systems, J. Am. Chem. Soc. 110, 8275-8287 (1988).

12.  B. D. Ray, R. M. Scheek, M. D. Kemple, F. G. Prendergast, and B. D. Nageswara Rao, Photochemically-Induced Dynamic Nuclear Polarization Proton NMR of Aequorin Discharged by Calcium-Independent Light Emission, Eur. J. Biochem. 178, 705-709 (1989).

13.  P. W. Rabideau, W. K. Smith, and B. D. Ray, Unusual Behavior of Isopropyl Substituents in 9,10-Dihydroanthracenes:  an NMR and Molecular Mechanics Study, Magn. Reson. Chem. 27, 191-196 (1989).

14.  A. J. Weaver, M. D. Kemple, and F. G. Prendergast, Characterization of Selectively 13 C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy, Biochemistry 28, 8614-8623 (1989).

15.  A. J. Weaver, M. D. Kemple, and F. G. Prendergast, Fluorescence and 13C NMR Determination of Side-Chain and Backbone Dynamics of Synthetic Melittin and Melittin Analogues in Isotropic Solvents, Biochemistry 28, 8624-8639 (1989).

16.  G. K. Jarori, B. D. Ray, and B. D. Nageswara Rao, 31P and 1H NMR Studies of the Structure of Enzyme-Bound Substrate Complexes of Lobster Muscle Arginine Kinase:  Relaxation Measurements with Mn(II) and Co(II), Biochemistry 28, 9343-9350 (1989).

17.  M. D. Kemple, M. L. Lovejoy, B. D. Ray, F. G. Prendergast, and B. D. Nageswara Rao, Mn(II)-EPR Measurements of Cation Binding by Aequorin, Eur. J. Biochem. 187, 131-135 (1990).

18.  B. D. Ray, J. M. Moore, and B. D. Nageswara Rao, 31P NMR Studies of Enzyme-Bound Substrate Complexes of Yeast 3-Phosphoglycerate Kinase:  3.  Two ADP Binding Sites and Their Mg(II) Affinity; Effects of Vanadate and Arsenate on Enzymic Complexes with ADP and 3-P-glycerate, J. Inorg. Biochem. 40, 47-57 (1990).

19.  S. B. Landy, B. D. Ray, P. Plateau, K. B. Lipkowitz, and B. D. Nageswara Rao, Conformation of MgATP Bound to Nucleotidyl and Phosphoryl Transfer Enzymes: 1H Transferred NOE Measurements on Complexes of Methionyl tRNA Synthetase and Pyruvate Kinase, Eur. J. Biochem. 205, 59-69 (1992).

20.  B. D. Nageswara Rao and B. D. Ray, 13C NMR Lineshapes of [2-13C]ATP in Enzyme Complexes and Viscous Solutions:  Glycosideic Rotation Persists at High Viscosities and Is Arrested in Enzyme Complexes, J. Am. Chem. Soc. 114, 1566-1573 (1992).

21.  A. J. Weaver, M. D. Kemple, J. W. Brauner, R. Mendelsohn, and F. G. Prendergast, Fluorescence, CD, Attenuated Total Reflectance (ATR) FTIR, and 13C NMR Characterization of the Structure and Dynamics of Synthetic Melittin and Melittin Analogues in Lipid Environments. Biochemistry 31, 1301-1313 (1992).

22.  N. Murali, G. K. Jarori, S. B. Landy, and B. D. Nageswara Rao. Two-Dimensional Transferred Nuclear Overhauser Effect Spectroscopy (TRNOESY) Studies of Nucleotide Conformations in Creatine Kinase Complexes:  Effects Due to Weak Nonspecific Binding, Biochemistry 32, 12941-12948 (1993).

23.  M. D. Kemple, K. E. Nollet, P. Yuan, and F. G. Prendergast, "Active-Site" Dynamics: A Comparison of the Wild Type and Single Tryptophan Variants of E. Coli Thioredoxin, Techniques in Protein Chemistry IV (R. H. Angeletti, ed.), pp. 595-603 Academic Press, New York (1993).

24.  P. Buckley, A. S. Edison, M. D. Kemple, and F. G. Prendergast, 13C-NMR Assignments of Melittin in Methanol and Chemical Shift Correlations with Secondary Structure, J. Biomol. NMR 3, 639-652 (1993).

25.  M. D. Kemple, P. Yuan, K. E. Nollet, J. A. Fuchs, N. Silva, and F. G. Prendergast, 13C NMR and Fluorescence Analysis of Tryptophan Dynamics in Wild-Type and Two Single-Trp Variants of Escherichia coli Thioredoxin, Biophys. J. 66, 2111-2126 (1994).

26.  G. K. Jarori, N. Murali, and B. D. Nageswara Rao, Two-Dimensional Transferred Nuclear Overhauser Effect Spectroscopy Study of the Conformation of MgATP Bound at the Active and Ancillary Sites of Rabbit Muscle Pyruvate Kinase, Biochemistry 33, 6784-6791 (1994).

27.  N. Murali, G. K. Jarori, and B. D. Nageswara Rao, Two-Dimensional Transferred Nuclear Overhauser Effect Spectroscopy (TRNOESY) Studies of Nucleotide Conformations in Arginine Kinase Complexes, Biochemistry 33, 14227-14236 (1994).

28.  L. Zhu, M. D. Kemple, S. B. Landy, and P. Buckley, Effect of Dipolar Cross Correlation on Model-Free Motional Parameters Obtained From 13C Relaxation in AX2 Systems, J. Magn. Reson. B 109, 19-30 (1995).

29.  L. Zhu, M. D. Kemple, P. Yuan, and F. G. Prendergast, N-Terminus and Lysine Side Chain pKa Values of Melittin in Aqueous Solutions and Micellar Dispersions Measured by 15 N NMR, Biochemistry 34, 13,196-13,202 (1995).

30.  P. Yuan, P. J. Fisher, F. G. Prendergast, and M. D. Kemple, Structure and Dynamics of Melittin in Lysomyristoyl Phosphatidylcholine Micelles Determined by NMR, Biophys. J. 70, 2223-2238 (1996).

31.  N. Murali, Y. Lin, Y. Mechulam, P. Plateau, and B. D. Nageswara Rao, Adenosine Conformations of Nucleotides Bound to Methionyl tRNA synthetase by Transferred Nuclear Overhauser Effect Spectroscopy, Biophys. J. 70, 2275-2284.

32.  B. D. Ray, M. H. Chau, W. K. Fife, G. K. Jarori, and B. D. Nageswara Rao, Conformation of Manganese(II)-Nucleotide Complexes Bound to Rabbit Muscle Creatine Kinase:   13C NMR Measurements Using [2-13C]ATP and [2-13C]ADP, Biochemistry 35, 7239-7246 (1996).

33.  M. D. Kemple, P. Buckley, P. Yuan, and F. G. Prendergast, Main Chain and Side Chain Dynamics of Peptides in Liquid Solution From 13C NMR:  Melittin as a Model Peptide, Biochemistry 36, 1678-1688 (1997).

34.  L. Zhu, F. G. Prendergast, and M. D. Kemple, Comparison of 15N- and 13C-Determined Parameters of Mobility in Melittin, J. Biomol. NMR 12, 135-144 (1998).

35.  L. Zhu, E. Kurian, F. G. Prendergast, and M. D. Kemple, Dynamics of Palmitic Acid Complexed With Rat Intestinal Fatty Acid Binding Protein, Biochemistry 38, 1554-1561 (1999).

36.  B. D. Ray, G. K. Jarori, and B. D. Nageswara Rao, Paramagnetic Effects on Nuclear Relaxation in Enzyme-Bound Co(II)-Adenine Nucleotide Complexes:  Relative Contributions of Dipolar and Scalar Interactions, J. Magn. Reson. 136, 130-133 (1999).

37.  D. Gachotte, S. E. Sen, J. Eckstein, R. Barbuch, M. Krieger, B. D. Ray, and M. Bard, Characterization of the Saccharomyces cerevisiae ERG27 Gene Encoding the 3-Keto Reductase Involved in C-4 Sterol Demethylation, Proc. Nat. Acad. Sci. (USA) 96, 12655-12660 (1999).

38.  V. Raghunathan, M. H. Chau, B. D. Ray, and B. D. Nageswara Rao, Structural Characterization of Manganese(II)-Nucleotide Complexes Bound to Yeast 3-Phosphoglycerate Kinase:  13C Relaxation Measurements Using [U-13C]ATP and [U-13C]ADP, Biochemistry 38, 15597-15605 (1999).

39.  B. D. Nageswara Rao, Characterization of Reaction Complex Structures of ATP-Utilizing Enzymes by High Resolution NMR, in M. Pons, Ed., NMR in Supramolecular Chemistry, pp. 155-170, Kulwer Academic, The Netherlands (1999).

40.  B. D. Nageswara Rao, How Far Does the Itinerant Phosphoryl Group Move on a Phosphoryl-Transfer Enzyme, Phosphorous, Sulfur and Silicon 144-146, 309-312 (1999).

41.  K. Konno, K. Ue, M. Khoroshev, H. Martinez, B. Ray, and M.F. Morales, Consequences of Placing an Intramolecular Crosslink in Myosin S1, Proc. Natl. Acad. Sci. (USA) 97 , 1461-1466 (2000).

42.  Y. Lin, and B. D. Nageswara Rao, Structural Characterization of Adenine Nucleotides Bound to E. coli Adenylate Kinase. 1. Adenosine Conformations by Proton Two Dimensional Transferred Nuclear Overhauser Effect Spectroscopy, Biochemistry 39, 3636-3646 (2000).

43.  Y. Lin, and B. D. Nageswara Rao, Structural Characterization of Adenine Nucleotides Bound to E. coli Adenylate Kinase. 2. 31P and 13C Relaxation Measurements in the Presence of Co(II) and Mn(II), Biochemistry 39, 3647-3655 (2000).

44.  P. C. Sanghani, C. L. Stone, B. D. Ray, E. V. Pindel, T. D. Hurley, and W. F. Bosron, Kinetic Mechanism of Human Glutathione-Dependent Formaldehyde Dehydrogenase, Biochemistry 39, 10720-10729 (2000).

45.  G. D. Rosengerg, W. W. Hughes, D. L. Parker, and B. D. Ray, The Geometry of Bivalve Shell Chemistry and Mantle Metabolism, Am. Malacolog. Bull. 16, 251-261 (2001).

46.  B. D. Ray, G. K. Jarori, and B. D. Nageswara Rao, Quantitation of Movement of the Phosphoryl Group During Catalytic Transfer in the Arginine Kinase Reaction : 31P Relaxation Measurements on Enzyme-Bound Equilibrium Mixtures, J. Biomol. NMR 23, 13-21 (2002).

47.  B. D. Ray, M. I. Khoroshev, K. Ue, Manuel F. Morales, and B. D. Nageswara Rao, Changes in the 31P NMR Spectrum of Rabbit Muscle Myosin Subfragment-1•MgADP with Temperature, Arch. Biochem. Biophys. 402, 243-248 (2002).

48.  Y.-Y. Fang, B. D. Ray, C. A. Claussen, K. B. Lipkowitz and E. C. Long, Ni(II)-Arg-Gly-His—DNA Interactions:  Investigation into the Basis for Minor-Groove Binding and Recognition, J. Am. Chem. Soc. 126, 5403-5412 (2004).

49.  B. D. Ray, G. K. Jarori, V. Raghunathan, H. Yan, and B. D. Nageswara Rao, Conformations of Nucleotides bound to Wild Type and Y78F Mutant Yeast Guanylate Kinase: Proton Two-Dimensional Transferred NOESY Measurements, Biochemistry 44, 13762-13770 (2005).

49.  B. D. Ray, J. Scott, H. Yan, and B. D. Nageswara Rao, Productive versus Unproductive Nucleotide Binding in Yeast Guanylate Kinase Mutants: Comparison of R41M with K14M by Proton Two Dimensional Transferred NOESY, Biochemistry 48, 5532-5540 (2009).