Ron Venters



Ronald A. Venters

Box 3711
Duke University Medical Center
Durham, NC  27710
Work Phone: (919)-613-8888  Fax: (919)-684-8885
e-mail: venters@duke.edu

Education

Butler University, B.S. 1980, Chemistry.
Northwestern University, M.S. 1981, Chemistry.
Northwestern University, Ph.D. 1985, Physical Chemistry.

Professional Experience

Research Chemist, E.I. DuPont de Nemours, 1985-87
Visiting Scientist, Duke University Medical Center, 1987-89
Associate Director of Serology, Roche Biomedical Laboratories, 1987-89
Postdoctoral Associate, Duke University Medical Center, 1989-90
Senior Spectroscopist, Duke University NMR Center, 1990-2008
Associate Director, Duke University NMR Center, 2008-present
Visiting Scientist with Dr. Lewis Kay, University of Toronto, 1998-1999

Professional Societies

American Chemical Society, American Association for the Advancement of Science, Protein Society

Publications

Hoffman, B.M., Venters, R.A. and Roberts, J.E. (1982), J. Amer. Chem. Soc104:4711.  57Fe ENDOR of Nitrogenase MoFe Protein.

Cline, J., Reinhammer, B., Jensen, P. and Venters, R.A. (1983), J. Biol. Chem258(8):5124.  Coordination Environment for the Type 3 Copper Center of Tree Laccase and CopperB of Cytochrom c Oxidase as Determined by Electron Nuclear Double Resonance.

Hoffman, B.M., Martinsen, J. and Venters, R.A. (1984), J. Magn. Reson59:110. General Theory of Polycrystalline ENDOR Patterns: the g and Hyperfine Tensors of Arbitrary Symmetry and Relative Orientation.

Venters, R.A., Anderson, J.R.,Cline, J.F. and Hoffman, B.M. (1984), J. Magn. Reson58:507.  ENDOR with a Loop-Gap Resonator.

Hoffman, B.M., Venters, R.A. and Martinsen, J. (1985), J. Magn. Reson65:537. General Theory of Polycrystalline ENDOR Patterns: Effects of Finite EPR and ENDOR Component Linewidths.

Anderson, J.R., Venters, R.A., Bowman, M.K., True, E.A. and Hoffman B.M. (1985),J. Magn. Reson. 65:165.  ESR and ENDOR Applications of Loop-Gap Resonators with Distributed Circuit Coupling.

Venters, R.A., Nelson, M.J., McLean, P.A., True, A.E., Levy, M.A., Hoffman, B.M.and Orme-Johnson, W.H. (1986), J. Amer. Chem. Soc. 108:3487.  ENDOR of the Resting State of Nitrogenase Molybdenum-Iron Proteins from Azotobacter vinelandii, Klebsiella pneumoniae and Clostridium pasteurianum1H, 57Fe, 95Mo and 33S Studies.

True, A.E., Nelson, M.J., Venters, R.A., Orme-Johnson, W.H. and Hoffman, B.M. (1988), J. Amer. Chem. Soc. 110:1935.  57Fe Hyperfine Coupling Tensors of the FeMo Cluster in Azotobacter vinelandii MoFe Protein: Determination by Polycrystalline ENDOR Spectroscopy.

Hoffman, D.W., Venters, R.A., Shedd, S.F. and Spicer, L.D. (1990), Magn. Reson. in Med. 13(3):507.  Use of Gel Filtration in the Preparation of Biological Fluids for Magnetic Resonance Spectroscopy.

Venters, R.A., Calderone, T.L., Spicer, L.D. and Fierke, C.A. (1991), Biochemistry30:4491.  Uniform 13C Isotope Labeling of Proteins with Sodium Acetate for NMR Studies:  Application to Human Carbonic Anhydrase II.

Fierke, C.A., Krebs, J.F. and Venters, R.A. (1991), Proceedings, International Workshop on Carbonic Anhydrase, Verlag-Chemie, Heidelberg.  From Biochemistry and Genetics to Physiology and Clinical Medicine.

Farmer II, B.T., Venters, R.A., Spicer, L.D., Wittekind, M.G. and Mueller, L. (1992), J. Biomol. NMR 2:195.  A Refocused and Optimized HNCA: Increased Sensitivity and Resolution in Large Macromolecules.

Venters, R.A. and Spicer, L.D. (1995), Techniques in Protein Chemistry VI, J.W. Crabb, ed., Academic Press, San Diego, p. 495. Heteronuclear Gradient-Enhanced NMR for the Study of 20-30kDa Proteins:  Application to Human Carbonic Anhydrase II.

Brown, R.A., Venters, R.A., Peng-Peng, P.Z.T. and Spicer, L.D. (1995), J. Mag. Reson., 113:117.  A Test for Scalar Coupling between Heteronuclei Using Gradient-Enhanced Protein-Detected HMQC Spectroscopy.

Farmer II, B.T. and Venters, R.A. (1995), J. Am. Chem. Soc. 117:4187.  Assignment of Sidechain 13C Resonances in Perdeuterated Proteins.

Venters, R.A., Huang, C-C., Farmer II, B.T., Trolard, R., Spicer, L.D. and Fierke, C. (1995), J. Biomol. NMR5:339.  High-level2H/13C/15N Labeling of Proteins for NMR Studies.

Venters, R.A., Metzler, W.J., Spicer, L.D., Mueller, L. and Farmer II, B.T. (1995), J. Am. Chem. Soc117:9592.  Use of 1HN1HNNOEs to Determine Protein Global Folds in Perdeuterated Proteins.

Farmer II, B.T. and Venters, R.A. (1996) J. Biomol. NMR7:59.  Assignment of Aliphatic Sidechain 1HN/15N Resonances in Perdeuterated Proteins.

Venters, R.A., Farmer II, B.T., Fierke, C.A., and Spicer, L.D. (1996) J. Mol. Biol., 264:1101.  Characterizing the use of perdeuteration in NMR studies of large proteins: 13C, 15N, and 1H assignments of human carbonic anhydrase II.

Venters, R.A., Vu, H.M., de Lormier, R.M., and Spicer, L.D. (1997), Techniques in Protein Chemistry VIII, D.R. Marshak, ed., Academic Press, San Diego, p. 605.  Strategies for NMR Assignment and Global Fold Determinations Using perdeuterated Proteins.

Luck, L.A., Venters, R.A., Kapron, J.T., Roth, K.E., Barrows, S.A., Paradis, S.G., and Crabb, J.W. (1997), Techniques in Protein Chemistry VIII, D.R. Marshak, ed., Academic Press, San Diego, p. 439.  NMR Methods for Analysis of CRALBP Retinoid Binding.

Venters, R.A., Farmer II, B.T. (1998) Invited chapter for Biological Magnetic Resonance.  (Berliner, L.J.,ed) Vol. 16, Plenum Press, NY.  NMR of Perdeuterated Large Proteins.

Yang, D., Venters, R.A., Mueller, G.A., Choy, W.Y. and Kay, L.E. (1999) J. Bio. NMR 14:333. TROSY-based HNCO Pulse Sequences for the Measurement of 1HN15N, 15N-13CO, 1HN13CO, 13CO-13CA and 1HN13CA.

Mueller, G.A., Choy, W.Y., Yang, D., Forman-Kay, J.D., Venters, R.A. and Kay, L.E. (2000) J. Mol. Biol. 300:197.  Global Folds of Proteins Using Residual Dipolar Couplings: Application to the 370 Residue Maltodextrin Binding Protein.

Cavanagh, J., Venters, R.A. (2001) Nat Struct Biol. 8(11):912-4.  Protein dynamic studies move to a new time slot.

Venters, R.A., Thompson, R. and Cavanagh, J. (2002), Invited manuscript for Journal of Molecular Structure 602-603:275-292. Current Approaches for the Study of Large Proteins by NMR.

Venters, R.A., Benson, L.M., Craig, T.A., Paul, K.H., Kordys, D.R., Thompson, R., Naylor, S., Kumar, R. and Cavanagh, J. (2003) J. Anal. Biochem317:59-66.  The effects of Ca 2+ binding on the conformation of calbindin D28K: An NMR and mESI-MS study.

Lutz, W., Frank, E.M, Thompson, R., Venters, R.A., Kojetin, D., Cavanagh, J. and Kumar, R. (2003), Biochem. Biophys. Res. Commun.303(4):1186-92.  Calbindin D28K Interacts with Ran-Binding Protein M..

Coggins, B.E., Venters, R.A. and Zhou, P. (2004), J. Am. Chem. Soc 126(4) :1000-1001. Generalized Reconstruction of n-D NMR Spectra from Multiple Projections: Application to the 5-D HACACONH Spectrum of Protein G B1 Domain.

Venters, R. A.; Coggins, B. E.; Kojetin, D.; Cavanagh, J.; Zhou, P. (2005), J Am Chem Soc.127, (24) , 8785-95. (4,2)D Projection-Reconstruction Experiments for Protein Backbone Assignment: Application to Human Carbonic Anhydrase II and Calbindin D28K .

Coggins, B. E.; Venters, R. A.; Zhou, P., (2005) J Am Chem Soc.127, (33) , 11562-3. Filtered Backprojection for the Reconstruction of a High-Resolution (4,2)D CH 3 -NH NOESY Spectrum of a 29 kDa Protein.

Bobay, B.G., Mueller, G.A., Thompso, R.J., Murzin, A.G., Venters, R.A., Strauch, M.A. and Cavanagh, J.(2006) J. Biol. Chem.281,21399-21409. NMR Structure of AbhN and Comparison with AbrBN: First Insights into DNA Binding Promiscuity and Specificity of AbrB-like Transition State Regulator Proteins.

Kojetin, D., Venters, R.A ., Thompson,R., Kordys, D., Kumar, R. and Cavanagh, J. (2006) Nat Struct Mol Biol 13, 641 -7. Structure, binding interface and hydrophobic transitions of Ca(2+)-loaded calbindin-D(28K).

Niranjanakumari S., Day-Storms J.J., Ahmed M., Hsieh J., Zahler N.H., Venters R.A . and Fierke C.A. (2007) RNA 13(4) , 521-535. Probing the architecture of the B. subtilis RNase P holoenzyme active site by cross-linking and affinity cleavage.

Kordys, D.R., Bobay, B.G.,Thompson, R.J., Venters, R.A. and Cavanagh, J. (2007) FEBS Lett 581(24) , 4778-82. Peptide binding proclivities of calcium loaded calbindin-D28K.

Kojetin, D.J., McLaughlin, P.D., Thompson, R.J., Venters, R.A. , Rance, M. and Cavanagh, J. (2007) Biomol NMR Assign , 163-165. NMR assignment of the N-terminal repeat domain of Bacillus subtilis ClpC.

Invited Lectures

37th Experimental NMR Conference (1996) Pacific Grove, California.  Protein Assignment and Global Fold Determination of Large2H/13C/15N Labeled Proteins.

38th Experimental NMR Conference (1997) Orlando, Florida.  Global Fold Determination of Perdeuterated Proteins: Conceptual Considerations.

University of Notre Dame Departments of Chemistry and Biochemistry Seminar Series (1998) Notre Dame, Indiana.  Protein Assignment and Global Fold Determination of Large 2H/13C/15N Labeled Proteins.

University of North Carolina Biochemistry Seminar Series (2000) Chapel Hill, NC.  NMR Studies of “Large” Proteins and Complexes.

University of Toronto Chemistry Seminar Series (2001) Toronto, Ontario.  Calcium Binding Proteins.

University of Georgia Complex Carbohydrate Research Center (2001) Athens, Georgia.  Assignment and Solution Structure Determination of Large Proteins and Complexes by NMR.

115th North Carolina American Chemical Society Sectional Conference (2001) Raleigh, North Carolina.  Calcium Binding Proteins.

20th International Conference on Magnetic Resonance in Biological Systems (2002) Toronto, Ontario.  Creative Dynamics in a Calcium Binding Protein.

Biomolecular NMR Workshop (2003) University of Alabama in Huntsville.  Assignments and Structures of Large Proteins and Complexes by NMR.

Southeast Collaboratory on Biological NMR (2006) University of Georgia in Athens. Projection-Reconstruction NMR: Experiments and Reconstruction Algorithms.

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