Graduate Programs in:
University of Montana
Levi J. McClelland, Biochemistry & Biophysics Graduate Student (Ph.D.)
"This is a great environment to live and work in and I have been fortunate to meet many great friends."
Levi is from Slippery Rock, PA and comes to UM from Slippery Rock University. He is currently working in Dr. Bowler's lab on his Ph.D. In his free time he enjoys recreating in Montana's great outdoors with his pup, Barley.
Research Focus: Cytochrome c: Residue effects on and regluation of protein dynamics
Facutly Advisor: Dr. Bruce Bowler
The use of thermodynamic and kinetic techniques to study conformational changes of proteins. Specifically, we make use of iso-1-cytochrome c to study the mechanisms in regulating conformational change, which contribute to protein function. Further we investigate contribution of residues to structure and relate our results to protein function including electron transfer and peroxidase activity, both of which are functions that cytochrome c undergoes during cellular energy production and the beginning steps of the intrinsic pathway of apoptosis, respectively.
Recent publication: McClelland, L. J., Mou, T. C., Jeakins-Cooley, M. E., Sprang, S. R. and Bowler, B. E. (2013) Structure of a mitochondrial cytochrome c conformer competent for peroxidase activity, submitted for publication.
Conferences: CBSD CoBRE Retreat 2012, 2013; NORM 2012, 2013; Biophysical Society 2013; MAS Spring 2013; Spring ACS (MT) 2013; UM Graduate Conference 2011-2013; ICBIC 15, 2011
Bruce Bowler, Professor
"I love the collaborative friendly environment of not just the research community at UM, but the Missoula community as a whole."
Dr. Bowler is the Biochemistry Graduate Program Director. He earned his Ph.D. from MIT, and currently is working with 3 graduate students. In his free time Bruce enjoys hiking with his Portuguese Water Dogs and singing tenor in the Missoula Symphony Chorale.
Research focus: Structural Studies on Alternate Conformers of Cytochrome c Required for Apoptosis (Programmed Cell Death)
The heme crevice loop of cytochrome c encloses one surface of the heme cofactor. The heme is essential for both the electron transport and apoptotic functions of this protein. The heme crevice loop is the most highly conserved segment of the sequence of cytochrome c with 13 of 16 amino acids identical between yeast and humans. It is clearly highly evolved to carry out the two functions of the protein. Levi and I are collaborating with the Sprang and Ross labs to dissect the role of particular amino acids in the heme crevice loop in controlling access of cytochrome c to alternate conformers needed for the peroxidation of the mitochondrial membrane lipid, cardiolipin, in the early stages of apoptosis. We have just submitted a manuscript which describes a new structural form of the cytochrome c made possible by mutation of a residue in the heme crevice loop. This mutation also increases the peroxidase activity of the protein.
Current research funding: National Science Foundation, NSF: Gatekeeper Residues Control Peroxidase Activity of Cytochrome c in Apoptosis
The structure-function paradigm, which indicates that proteins have a unique structure designed for a single function, dominates biochemistry textbooks. Recent work indicates that many proteins can access more than one structure allowing them to carry out multiple functions. Cytochrome c is involved in both the electron transport chain, the primary energy storage pathway in aerobic organisms, and in apoptosis (programmed cell death) a key process in the growth and development of higher organisms such as mammals. This research will provide a molecular level understanding of how the transition between the two structures needed to carry out these two functions is controlled in cytochrome c.
McClelland, L. J., Mou, T. C., Jeakins-Cooley, M. E., Sprang, S. R. and Bowler, B. E. (2013) Structure of a mitochondrial cytochrome c conformer competent for peroxidase activity, submitted for publication.
Cherney, M. M., Junior, C. C., Bergquist, B. B. and Bowler, B. E. (2013) Dynamics of the His79-heme alkaline transition of yeast iso-1-cytochrome c probed by conformationally gated electron transfer with Co(II)bis(terpyridine). J. Am. Chem. Soc. 135, 12772-12782. doi:10.1021/ja405725f
Cherney, M. M., Junior, 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
Featured Students and Faculty Archives
Five years after the building’s frame was completed, the Interdisciplinary Science Building is starting to fill in. ISB is undergoing construction to finish its basement, second floor and part of the fourth floor. The $3.28 million project is funded by overheads from grants awarded for research on campus, said associate Vice President of Administration and Finance Rosi Keller. With every research grant, money is awarded to the institution for future development of research space. (Read more)
Science Departments Collaborate on Graduate Program Resource Website for Students, September 5, 2013
Five UM departments and programs recently teamed up to create a resource website for potential and current graduate students in the biomedical, cellular, biochemical and chemical sciences. The site is a collaboration between the UM Department of Biomedical and Pharmaceutical Sciences, Division of Biological Sciences, the Department of Chemistry and Biochemistry, the Center for Biomolecular Structure and Dynamics, and the Graduate School.
The site offers students a one-stop shop to find information about programs, potential faculty mentors and the world-class research happening in these fields at UM. Previously, this information only could be found by visiting multiple department and program pages, as well as the main Graduate School website.
“We feel that this interdisciplinary website will help students find information and faculty contacts more seamlessly as they consider UM for their graduate studies,” said Cathy Jo Beecher, program coordinator for the UM Center for Biomolecular Structure and Dynamics.
The Graduate School hosts the new website under “Programs,” and it also is featured on the CBSD website under “Graduate Programs.” All three departments associated with the site will feature it as a resource on their webpages, as well.