Faculty

Bruce Bowler

Bruce Bowler

Professor and Director, Biochemistry Program

Office: Chem 311A
Email: bruce.bowler@umontana.edu
Office Hours:

Tuesdays and Thursdays 3:00 to 4:00 pm or by appointment

(Office entrance is through Chem 310)


Courses

BCH 294 Introductory Biochemistry Seminar

CHMY 401 Advanced Inorganic Chemistry

BCH 581 Physical Biochemistry

BCH 582 Proteins and Enzymes

Personal Summary

Bruce Bowler joined the University of Montana in 2006 as Professor of Chemistry and a member of the Center for Biomolecular Structure and Dynamics.  He received his Ph. D. degree in 1986 with Stephen J. Lippard at the Massachusetts Institute of Technology.  From 1986 to 1989, he was a Medical Research Council of Canada postdoctoral fellow in the laboratories of Harry Gray and Jack Richards at the California Institute of Technology.  From 1989 to 2006 he was a professor of chemistry at the University of Denver.  Dr. Bowler is a physical biochemist with interests in protein folding and biological electron transfer reactions.  Dr. Bowler is also the Director of the newly developed Biochemistry Program.

Research Interests

Research in the Bowler lab focuses on two areas: protein folding and the relationship between protein conformational dynamics and function. 

Our work on protein folding emphasizes the conformational biases inherent in protein denatured states that bias the free energy landscape of a protein toward its native conformer. The ultimate goal of this research is to understand the physical basis of the protein folding code.    

Our work on the relationship between protein conformational dynamics and function focuses on the structural factors that control access to conformers of mitochondrial cytochrome c  which permit peroxidase activity. Under conditions of oxidative stress cytochome c oxygenation of the inner mitochondrial membrane lipid, cardiolipin, provides the earliest signal in the intrinsic pathway of apoptosis. A key goal of this work is to understand how cytochrome c has evolved to become a regulatory on/off switch for apoptosis.

Selected Publications

McClelland, L.J., Steele, H. B. B., Whitby, F. G., Mou, T.-C., Holley, D., Ross, J. B. A., Sprang, S. R., and Bowler, B. E. (2016) Cytochrome c can form a well-defined binding pocket for hydrocarbons. J. Am. Chem. Soc. 138, 16770−16778. doi:10.1021/jacs.6b10745

McClelland, L. J., and Bowler, B. E. (2016) Lower protein stability does not necessarily increase local dynamics. Biochemistry 55, 2681–2693, doi:10.1021/acs.biochem.5b01060.

Goldes, M. E., Jeakins-Cooley, M. E.  McClelland, L. J., Mou, T.-C., and Bowler, B. E. (2016) Disruption of a hydrogen bond network in human versus spider monkey cytochrome c affects heme crevice stability. J. Inorg. Biochem. 158, 62-69, doi:10.1016/j.jinorgbio.2015.12.025

Stine, J. M., Sun, Y., Armstrong, G., Bowler, B. E., and Briknarová. K. (2015) Structure and Unfolding of the Third Type III Domain from Human Fibronectin. Biochemistry 54, 6724–6733.

McClelland, L. J., Seagraves, S. M, Khan, Md K. A., Cherney, M. M., Bandi, S., Culbertson, J. E. and Bowler, B. E. (2015) The response of Ω-loop D dynamics to truncation of trimethyllysine 72 of yeast iso-1-cytochrome c depends on the nature of loop deformation. J. Biol. Inorg. Chem. 20, 805-819. doi:10.1007/s00775-015-1267-1

Bandi, S., and Bowler, B. E., (2015) Effect of an Ala81His mutation on the Met80 loop dynamics of iso-1-Cytochrome c, Biochemistry 54, 1729-1742. doi:10.1021/bi501252z

McClelland, L. J., Mou, T. C., Jeakins-Cooley, M. E., Sprang, S. R. and Bowler, B. E. (2014) Structure of a mitochondrial cytochrome c conformer competent for peroxidase activity, Proc. Natl. Acad. Sci. USA 111, 6648-6653. doi:10.1073/pnas.1323828111

Cherney, M. M., Junior, C. C. and Bowler, B. E. (2013). Mutation of trimethyllysine-72 to alanine enhances His79-heme mediated dynamics of iso-1-cytochrome c. Biochemistry 52, 837-846. doi:10.1021/bi301599g

Bandi, S. and Bowler, B. E. (2013). A cytochrome c electron transfer switch modulated by heme ligation and isomerization of a peptidyl-prolyl bond. Biopolymers, Peptide Science 100, 114-124. doi:10.1002/bip.22164/abstract

 Khan, Md. K. A. and Bowler, B. E. (2012). Conformational properties of polyglutamine sequences in guanidine hydrochloride solutions. Biophys. J. 103, 1989-1999. doi:10.1016/j.bpj.2012.09.041

Khan, Md. K. A., Miller, A. L. and Bowler, B. E. (2012). Tryptophan stabilizes His-heme loops in the denatured state only when it is near a loop end. Biochemistry, in press doi:10.1021/bi300212a.

Finnegan, M. L. and Bowler, B. E. (2012). Scaling properties of glycine-rich sequences in guanidine hydrochloride solutions. Biophysical J. 102, 1969-1978.  doi:10.1016/j.bpj.2012.03.049

Bowler, B. E. (2012) Characterization of the denatured state. In Egelman, E. H, editor: Comprehensive Biophysics Vol 3, The folding of Proteins and Nucleic Acids, Daggett, V., volume editor, Oxford: Academic Press, pp. 72-114.

Bowler, B. E. (2012). Residual structure in unfolded proteins. Curr. Opin. Struct. Biol. 22, 4-13. doi:10.1016/j.sbi.2011.09.002

Bandi, S. and Bowler B. E.; (2011). Probing the dynamics of a His73-heme alkaline transition in a destabilized variant of yeast iso-1-cytochrome c with conformationally gated electron transfer. Biochemistry 50, 10027–10040. doi:10.1021/bi201082h

Cherney, M. M.; Bowler, B. E. (2011) Protein dynamics and function: making new strides with an old warhorse, the alkaline conformational transition of cytochrome c. Coord. Chem. Rev. 255, 664-677. doi:10.1016/j.ccr.2010.09.014

Dar, T. A., Schaeffer, R. D., Daggett, V. and Bowler, B. E. (2011) Manifestations of native topology in the denatured state ensemble of Rhodopseudomonas palustris cytochrome c’. Biochemistry 50, 1029-1041. doi:10.1021/bi101551h

Finnegan, M. L. and Bowler, B. E. (2010). Propensities of aromatic amino acids versus leucine and proline to induce residual structure in the denatured state ensemble of iso-1-cytochrome c. J. Mol. Biol. 493, 495-504 doi:10.1016/j.jmb.2010.09.004.

Tzul, F. O. and Bowler, B. E. (2010). Denatured states of low complexity polypeptide sequences differ dramatically from those of foldable sequences. Proc. Natl. Acad. Sci. U.S.A.107, 11364-11369 doi:10.1073/pnas.1004572107.

Publications

Complete list of publications.