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Amanda N. Barry

Amanda Barry

Capabilities

  • Biosciences
  • Algal biofuels
  • Metabolomics
  • Proteomics
  • Microbial biochemistry

Expertise

Molecular biology and biochemistry - Mutagenesis, expression, and purification of proteins in eukaryotic and prokaryotic cells.

Manipulation of microalgae - Developing an efficient strategy for microalgae harvesting for biofuel production; Manager of the photobioreactor matrix at LANL.

Metal metabolism - Utilized X-ray absorption spectroscopy and a unique selenocysteine probe to determine the copper cluster in the copper chaperone for superoxide dismutase;  Identified and characterized a methionine and histidine-rich insert involved in copper binding in the copper-transporting ATPase, ATP7A.

Education

Ph.D., Biochemistry and Molecular Biology, Oregon Health & Science University, 2007

M.S., Bacteriology, University of Wisconsin-Madison, 2002

B.S., Biochemistry and Biophysics, Oregon State University, 1999

B.S., Bioresource Research, Oregon State University, 1999
 

 

LANL Positions

Postdoctoral Research Associate 1/2012 - present

 

Awards

JHPDA Highly Commended Poster and Presentation, Spring, 2011

Ruth L. Kirschstein National Research Service Award, 2008 - 2011

Igor Stojiljkovic Memorial Fellowship for Bioscience, 2006

Charles Patrick Memorial Fund Award, 2002

Powis Lee and Winifred Carlos Heitmeyer Scholarship, 1998

Oregon State University Research Office Summer Research Grant, 1998

DB DeLoach Scientific Study Grant, 1998

Richard Chambers Environmental Grant, 1997

Oregon State University Honors College, 1996 - 1999

 

Publications

 

Subramanian, S., Barry, A.N., Pieris, S., and Sayre, R.T. 2013. Comparative energetics and kinetics of autotrophic lipid and starch metabolism in chlorophytic microalgae: implications for biomass and biofuel production. Biotechnology for Biofuels 6(1):150.

Barry, A.N., Negi, S., Appuhamilage, N.S., Subramanian, S., Friedland, N., Pieris, S., Schaub, T., and Sayre, R.T. Impact of nitrogen limitation on biomass, photosynthesis, and lipid accumulation in Chlorella sorokiniana using a pond-simulated environment [In preparation]

Hatori, Y., Clasen, S., Hasan, N.M., Barry, A.N., and Lutsenko, S. 2012. Functional partnership of the copper export machinery and glutathione balance in human cells. J Biol Chem 287(32):26678-87

Otoikhian, A.A., Barry, A.N., Mayfield, M., Nilges, M.J., Huang, Y., Lutsenko, S., and Blackburn, N.J. 2012. The Lumenal Loop M672-P707 of the Menkes Protein (ATP7A) Transfers Copper to Peptidylglycine Monooxygenase. J Am Chem Soc 134(25):10458-68.

Barry, A.N., Otokhian, A., Bhatt, S., Shinde, U., Blackburn, N., and Lutsenko, S. 2011. The lumenal loop M672-P707 of copper-transporting ATPase ATP7A binds metals and facilitates copper release from the intramembrane sites. J Biol Chem 286(30):26585-94.

Barry, A.N., Shinde, U., and Lutsenko, S. 2010. Structural organization of human Cu-ATPases: Learning from building blocks. J Biol Inorg Chem 15(1):47-59.

Leshane, E.S., Shinde, U., Walker, J.M., Barry, A.N., Blackburn, N.J., Ralle, M., and Lutsenko, S. 2009. Interactions between copper-binding sites determine the redox status and conformation of the regulatory N-terminal domain of ATP7B. J Biol Chem 285(9):6327-36.

Barry, A.N., Akram, Z., and Lutsenko, S. 2010. Chapter 8: Mechanism of Human Copper Transporter Wilson’s Disease Protein in Protein Folding and Metal Ions: Mechanisms, Biology and Disease. CRC Press.

Barry A.N., Clark, K.M., Otoikhian, A., van der Donk, W.A., and Blackburn, N.J.  2008. Selenocysteine positional variants reveal contributions to copper binding from cysteine residues in domains 2 and 3 of human copper chaperone for superoxide dismutase. Biochem 47(49):13074-83. 

Barry, A.N. and Blackburn, N.J. 2008. A Selenocysteine Variant of the Human Copper Chaperone for Superoxide Dismutase.  A Se-XAS probe of Cluster Composition at the Domain 3-Domain 3 Dimer Interface. Biochem 47(17):4916-28.

Stasser, J.P., Barry, A.N., and Blackburn, N.J. A Multinuclear Copper (I) Cluster Forms the Dimerization Interface in Copper-loaded Human Copper Chaperone for Superoxide Dismutase. Biochem 46(42):11845-56.

Himes, R.A., Park, G.Y., Barry, A.N., Blackburn, N.J., and Karlin, K.D. 2007. Synthesis and X-ray Absorption Spectroscopy Structural Studies of Cu(I) Complexes of HistidylHistidine Peptides: The Predominance of Linear 2-Coordinate Geometry. J Am Chem Soc 129(17):5352-3.

Stasser, J.P., Eisses, J.F., Barry, A.N., Kaplan, J.H., and Blackburn, N.J. 2005. Cysteine-to-serine mutants of the human copper chaperone for superoxide dismutase reveal a copper cluster at a domain III dimer interface. Biochem 44(9):3143-52.