Bruce Bowler

Bruce Bowler
Professor

Email: bruce.bowler@umontana.edu

Phone: (406) 243-6114

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.  Bruce Bowler is a physical biochemist with interests in protein folding and biological electron transfer reactions.

 

Research Interests

Research in the Bowler lab focuses on two areas: protein folding and electron transfer reactions in proteins and peptides.  Currently, work on protein folding centers on understanding the conformational properties of denatured states that provide for efficient folding and on the molecular basis of the cooperative stability of proteins.  Insight into these aspects of protein folding will shed light on the causes of protein misfolding and aggregation which can lead to pathological conditions such as Alzheimer’s disease and cystic fibrosis.    

Electron transfer reactions involving proteins are essential to the metabolism of all living organisms and are particularly important in photosynthesis in plants and energy storage in animals.  We are interested in understanding how the protein matrix, particularly hydrogen bond networks, modulates the rates of electron transfer reactions. We are also exploiting protein conformational changes as a means of creating molecular switches that can turn electron flow on and off and ultimately be used as components of molecular electronics devices.

The Bowler lab uses site-directed mutagenesis as a tool to create protein variants for these studies.  We then characterize the thermodynamic and structural properties of these variants using electronic, fluorescence, circular dichroism, NMR and mass spectroscopies.  The kinetic and dynamic properties of these variants are probed using stopped and continuous flow methods and limited proteolysis techniques.

Representative Publications

Bowler, B.E. (2008). Thermodynamic approaches to understanding protein denatured states. Unfolded proteins: from denatured state to intrinsically disordered (Creamer, T. P, Ed.), in press.

Bandi, S., Baddam, S., and Bowler, B.E. (2007). The alkaline conformational transition and gated electron transfer with a Lys 79 > His variant of iso-1-cytochrome c. Biochemistry 46, 10643-10654.

Tzul, F. O., Kurchan, E., and Bowler, B.E. (2007). Sequence composition effects on denatured state loop formation in islo-1-cytochrome c variants: Polyalanine versus polyglycine inserts. J. Mol. Biol. 371, 577-584.

Bowler, B. E. (2007). Thermodynamics of protein denatured states. Mol. BioSys., 3. 88-89.

Baddam, S., and Bowler, B. E. (2006). Tuning the rate and pH accesibility of conformational electron transfer gates.  Inorg. Chem. 45, 6338-6346.

Baddam, S., and Bowler, B. E. (2006). Mutation of Asn 52 to Gly promotes the alkaline form of iso-1-cytochrome c and causes loss of cooperativity in acid unfolding. Biochemistry 45, 4611-4619.

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