Christopher M. Bruns, Ph.D.

curriculum vitae

Mailing address:
The Scripps Research Institute, MB4
10550 N. Torrey Pines Rd.
La Jolla, CA 92037

E-mail: bruns@scripps.edu

Web page: http://www.scripps.edu/~bruns/

CONTENTS

EDUCATION

Ph.D. in Biochemistry, Molecular, and Cell Biology from Cornell University, Ithaca, New York; minor in Computer Science.

B.A. in Biology from Reed College, Portland, Oregon

High school: Sandy Spring Friends School, Sandy Spring, Maryland

[Cornell diploma] [Reed diploma]

PROFESSIONAL EXPERIENCE

Bioinformatics:

(Senior Scientist, Incyte Genomics) Designed and implemented methods for automated functional annotation of gene transcripts, coding region detection, and visualization of similarities between novel genes and known protein structures.

Structural Biology:

(Research Associate, The Scripps Research Institute) Solved crystal structures of iron transport proteins and glutathione transferases from pathogenic organisms. Developed software for the incorporation of atomic structure information into sequence alignment and molecular phylogeny calculations. Supervisor: John Tainer. Also worked closely with Duncan McRee, Elizabeth Getzoff, and Dave Stout.

(Graduate Student, Cornell University) Studied Photosynthetic electron/energy transfer. Extensively refined ferredoxin reductase crystal structure. Solved other crystal forms by molecular replacement. Solved mutant, ligand bound, and chemically modified structures by difference Fourier followed by refinement. Aligned sequences and structures for a large family of related proteins, evaluating conserved features in light of the atomic structure. Advisor: professor P.A. Karplus.

Molecular Biology/Cytology:

(Research Group Leader, DIGENE Diagnostics, Silver Spring, MD) Created and developed a rapid non-radioactive diagnostic test for papillomavirus infection on Pap smears, visible in individual cells using in situ DNA hybridization, as an early test for cancer probability. Also developed techniques involving enzyme kinetics, photo/video microscopy, and mammalian tissue culture. Immediate superior: CEO Floyd Taub, M.D.

Cellular/Neurobiology:

(Research Assistant/Senior Thesis, Reed College) Studied protein sorting and targeting. Dissected subcellular localization of radio-labeled peptides in Aplysia neurosecretory cells using pulse/chase protocols, subcellular fractionation, enzyme assays, and isoelectric focusing. Advisor: professor Stephen Arch

Computer Programming/Systems Administration:

Programming Accomplishments: 20 years programming experience. Several 3D/stereoscopic graphics projects. Biological sequence and 3D protein structure comparison. Many types of scientific data analysis.

Programming Languages: C, C++, JAVA, PERL, FORTRAN, PASCAL, BASIC, Assembly(6502).

Systems Administrator: (Cornell University)

Extensive experience with other platforms: Windows/MSDOS, Amiga, Apple II, Macintosh.

HONORS

MEMBERSHIPS

OTHER INTERESTS

Drawing and Painting, Juggling, Backpacking, Chess

PUBLICATIONS AND PRESENTATIONS

Articles:

  1. C.M. Bruns, I. Hubatsch, M. Ridderström, B. Mannervik, and J.A. Tainer (1999) Human Glutathione Transferase A4-4 Crystal Structures and Mutagenesis Reveal the Basis of High Catalytic Efficiency with Toxic Lipid Peroxidation Products. Journal of Molecular Biology 288(3): 427-439 [PubMed link]
    See also May 7, 1999 cover of Journal of Molecular Biology

  2. C.M. Bruns, A.J. Nowalk, A.S. Arvai, M.A. McTigue, K.G. Vaughan, T.A. Mietzner, and D.E. McRee (1997) Structure of Haemophilus influenzae Fe+3-binding Protein Reveals Convergent Evolution Within a Superfamily. Nature Structural Biology 4(11): 919-924.
    See also the "News and Views" companion piece: E.N. Baker (1997) Iron-ic twists of fate. Nature Structural Biology 4(11): 869-871.

  3. A. Aliverti, C.M. Bruns, V. E. Pandini, P. A. Karplus, M. A. Vanoni, B. Curti, and G. Zanetti (1995) Involvement of Serine 96 in the Catalytic Mechanism of Ferredoxin-NADP+ Reductase: Structure-Function Relationship as Studied by Site-Directed Mutagenesis and X-ray Crystallography. Biochemistry 34(26): 8371-8379

  4. C.M. Bruns and P.A. Karplus (1995) Refined Crystal Structure of Spinach Ferredoxin-NADP+ Reductase at 1.7Å Resolution: Oxidized, Reduced, and 2'-phospho-5'-AMP Bound States. Journal of Molecular Biology 247(1): 125-145

  5. C.M. Bruns and P.A. Karplus (1995) The Multi-drop Approach: More Efficient Screening of Crystallization Conditions. Journal of Applied Crystallography 28(2): 242-243

  6. * P.A. Karplus and C.M. Bruns (1994) Structure Function Relations for Ferredoxin Reductase. J. Bioenerg. Biomembr. 26(1): 89-99

  7. * C.M. Bruns and P.A. Karplus (1994) Refined Structures of Native, Complexed, and Reduced Forms of Spinach Ferredoxin Reductase. In: Flavins and Flavoproteins 1993 Ed.: K. Yagi., Walter de Gruyter and Co., Berlin pp. 443-445

  8. C.C. Correll, M.L. Ludwig, C.M. Bruns, and P.A. Karplus (1993) Structural Prototypes for an Extended Family of Flavoprotein Reductases: Comparison of Phthalate Dioxygenase Reductase with Ferredoxin Reductase and Ferredoxin. Protein Science 2(12): 2112-2133

  9. * C.M. Bruns and P.A. Karplus (1991) Evaluation of Secondary Structure Predictions for Enzymes Related to Ferredoxin Reductase. In: Flavins and Flavoproteins 1990 Eds.: B. Curti, S. Ronchi, and G. Zanetti. Walter de Gruyter and Co., Berlin pp. 487-490

  10. * F.E. Taub, S.L. Grillo, C. M. Bruns, N. Moore, and M.E. Mosher (1988) The Use of DNA Probes to Diagnose Viral Infections. Developments in Industrial Microbiology 29: 119-129

  11. S. Molloy, C. Bruns, and S. Arch (1987) Dissimilar Associations of Two Secretory Peptides with a Granule-enriched Fraction from the Bag Cells. Peptides 8(5): 829-836

('*' indicates invited articles and reviews)

Posters:

  1. C.M. Bruns and J.A. Tainer (1999) Multiple Sequence Alignment Using Both Sequences and Atomic Coordinates. Presented at the 14th West Coast Protein Crystallography Workshop, Asilomar conference center, Asilomar, California. March 14-17, 1999

  2. I. Hubatsch, M. Ridderström, C. Bruns, A.-S. Jonsson, J.A. Tainer, and B. Mannervik (1998) Human Glutathione Transferase A4-4: an Enzyme with high specificity for 4-hydroxynonenal. Presented at the meeting of the Swedish Biochemical Society.

  3. C.M. Bruns, K.G. Vaughan, A.J. Nowalk, T.A. Mietzner, and D.E. McRee (1998) Large-scale Conformational Change Upon Ligand Binding in Bacterial Fe+3 Binding Protein. Presented at the 1998 annual meeting of the American Crystallographic Association (ACA), Arlington, Virginia, July 18-23, 1998

  4. C.M. Bruns, A.J. Nowalk, A.S. Arvai, M.A.McTigue, T.A. Mietzner, and D.E. McRee (1997) Crystal Structure of Haemophilus Ferric-binding Protein: Insights into the Evolution of the Transferrin Superfamily. Presented at the West Coast Protein Crystallography Workshop, Asilomar conference center, Asilomar, California. March 15-19, 1997

  5. C.M. Bruns, A.S. Arvai, A.J. Nowalk, T.A. Mietzner, D.E. McRee, and J.A. Tainer (1996) Structure Analysis of Key Drug Design Target Enzymes from Human Pathogens. Presented at the meeting of the International Union of Crystallography, Seattle, Washington, August 8-17, 1996.

  6. C.M. Bruns and P.A. Karplus (1994) Assessing Significance of Protein Sequence Alignments for Structurally Known Proteins. Presented at the Meeting on the Critical Assessment of Techniques for Protein Structure Prediction. Asilomar conference center, Asilomar, California. December 4-8, 1994

  7. C.M. Bruns and P.A. Karplus (1993) Refined Structures of Native, Complexed, and Reduced Forms of Spinach Ferredoxin Reductase. Presented at the 11th International Symposium on Flavins and Flavoproteins, Nagoya, Japan, July 25-August 1, 1993

  8. C.M. Bruns and P.A. Karplus (1993) Sequence/structure Relationships in Enzymes Related to Ferredoxin Reductase. Presented at the 3rd annual Beckman Institute Symposium on Protein Structure and Function, Urbana/Champaign, Illinois, June 3-6, 1993

  9. C.M. Bruns and P.A. Karplus (1992) Refined Crystal Structure of Spinach Ferredoxin Reductase at 1.7Å Resolution. Presented at the 1992 meeting of the American Crystallographic Association (ACA), University of Pittsburgh, Pittsburgh, Pennsylvania, July, 1992

  10. C.M. Bruns and P.A. Karplus (1990) Evaluation of Secondary Structure Predictions for Enzymes Related to Ferredoxin Reductase. Presented at the 10th International Symposium on Flavins and Flavoproteins, Como, Italy, July 15-20, 1990

  11. C.M. Bruns, C.R. Ceccarelli, J. Summerville, T. Higgs, and F.E. Taub (1989) Type-specific HPV Detection in Pap Smears by in situ Hybridization with Enzyme-DNA Conjugates. Presented at the 8th International Papillomavirus Workshop. Taos, New Mexico, March, 1989. (abstract in) Journal of Cellular Biochemistry Supplement 13C, p.182.

  12. T. Higgs, N. Moore, G. Gamerman, C. Bruns, D. Badawi, and F.E. Taub (1989) Highly Sensitive, Rapid and Specific Detection of HPV types 6/11 and 16/18 in Formalin Fixed Paraffin Embedded Sections Using Directly Conjugated HRP Labeled Probes. Presented at the 8th International Papillomavirus Workshop. Taos, New Mexico, March, 1989. (abstract in) Journal of Cellular Biochemistry Supplement 13C, p.187.

  13. C.M. Bruns, C. Cardozo, C.R. Ceccarelli, L. Corey, J.M. Douglas, S.L. Grillo, A. Langenberg, J. Saba, and F.E. Taub (1988) Rapid in situ Hybridization to HPV Sequences in Cervical Smears Using Direct Enzyme-labeled DNA Probes. Presented at the 7th International Papillomavirus Workshop, Sophia Antipolis Côte d'Azur, France, May 1988

  14. S. Grillo, C. Bruns, M. Mosher, and F. Taub (1987) The Use of Direct DNA-peroxidase Conjugates for Rapid, Non-radioactive Detection of HPV Sequences by in situ Hybridization. Presented at the 6th International Papillomavirus Workshop, Georgetown University, Washington, D.C., July 1987

Invited Presentations:

  1. Structure and Evolution of Bacterial Fe+3-binding Protein. December 1996. Pathogenesis Affinity Group Lecture Series. The Scripps Research Institute. La Jolla, California

  2. Structure and Function of Spinach Ferredoxin Reductase. April 14, 1995. Department of Molecular Biology. The Scripps Research Institute. La Jolla, California

  3. Structure and Function of Spinach Ferredoxin Reductase. March 20, 1995. Department of Biochemistry. Medical College of Wisconsin. Milwaukee, Wisconsin. Includes 3D slide presentation.

Deposited Atomic Coordinates/Structure Factors:

(available from the Protein Data Bank)

  1. 1D9V: Coordinates and structure factors of apo (iron-free) H. influenzae bacterial transferrin at 1.75 Å resolution.

  2. 1D9Y: Coordinates and structure factors of N. gonorrhoeae bacterial transferrin at 2.20 Å resolution.

  3. 1GUL: Coordinates and structure factors of human brain glutathione transferase A4-4 bound to the inhibitor iodobenzyl glutathione at 2.7 Å resolution.

  4. 1GUM: Coordinates and structure factors of human brain apo glutathione transferase A4-4 at 3.0 Å resolution.

  5. 1MRP: Coordinates and structure factors of H. influenzae Fe+3-binding protein at 1.6 Å resolution.

  6. 1FRN: Coordinates and structure factors of spinach ferredoxin reductase with active site residue Ser96 mutated to Val at 2.0 Å resolution.

  7. 1FNC: Coordinates of chemically reduced spinach ferredoxin reductase at 1.7 Å resolution.

  8. 1FND: Coordinates of spinach ferredoxin reductase bound to the inhibitor 2',5'-ADP, an NADP fragment, at 1.7 Å resolution.

  9. 1FNB: Coordinates of native spinach ferredoxin reductase at 1.7 Å resolution.

Acknowledgments:

Chris Bruns is acknowledged for his contributions in the following publications:

  1. C.D. Putnam, M.J.N. Shroyer, A.J. Lundquist, C.D. Mol, A.S. Arvai, D.W. Mosbaugh, and J.A. Tainer (1999) Protein mimicry of DNA from crystal structures of the uracil-DNA glycosylase inhibitor protein and its complex with Escherichia coli uracil-DNA glycosylase. Journal of Molecular Biology 287(2):331-346

  2. G.S. Prasad, N. Kresge, A.B. Muhlberg, A. Shaw, Y.S. Jung, B.K. Burgess, and C.D. Stout (1998) The crystal structure of NADPH:ferredoxin reductase from Azotobacter vinelandii. Protein Science 7: 2541-2549

  3. Mol, C.D., Parikh, S. S., Lo, T. P. and Tainer, J. A. (1998) Structural Phylogenetics of DNA Base Excision Repair. In: Nucleic Acids and Molecular Biology, Vol. 12 (F. Eckstein and D.M.J. Lilley eds.) Springer-Verlag Berlin Heidelberg

  4. Y. Guan, M.J. Hickey, G.E.O. Borgstahl, R.A. Hallewell, J.R. Lepock, D. O'Connor, Y. Hsieh, H.S. Nick, D.N. Silverman, and J.A. Tainer (1998) Crystal Structure of Y34F Mutant Human Mitochondrial Superoxide Dismutase and the Functional Role of Tyrosine 34. Biochemistry 37(14): 4722-4730

  5. S.S. Parikh, C.D. Mol, and J.A. Tainer (1997) Base Excision Repair Enzyme Family Portrait: Integrating the Structure and Chemistry of an Entire DNA Repair Pathway. Structure 5: 1543-1550

  6. C.D. Mol, J.M. Harris, E.M. McIntosh, and J.A. Tainer (1996) Human dUTP Pyrophosphatase: Uracil Recognition by a Beta Hairpin and Active Sites Formed by Three Separate Subunits. Structure 4(9): 1077-1092

  7. G.S. Prasad, E.A. Stura, D.E. McRee, G.S. Laco, C. Hasselkus-Light, J.H. Elder, and C.D. Stout (1996) Crystal structure of dUTP Pyrophosphatase from Feline Immunodeficiency Virus. Protein Science 5(12): 2429-2437

  8. G.S. Prasad, D.E. McRee, E.A. Stura, D.G. Levitt, H.C. Lee, and C.D. Stout (1996) Crystal Structure of Aplysia ADP Ribosyl Cyclase, a Homologue of the Bifunctional Ectozyme CD38. Nature Structural Biology 3(11): 957-964

Academic Theses:

  1. C.M. Bruns (1995) The Structure of Spinach Ferredoxin Reductase. Ph.D. Thesis. Cornell University, Section of Biochemistry, Molecular and Cellular Biology, Ithaca, NY., May 1995

  2. C.M. Bruns (1986) Protein Processing in the Bag Cells of Aplysia. B.A. Thesis, Reed College Biology Department, Portland, OR

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