个人简介

Education Postdoctoral Fellow, University of Pennsylvania, 2006 PhD, Arizona State University, 2001 B.S. Humboldt State University, 1995 Honors and Awards 2005 Recognition of Outstanding Research American Heart Association (AHA) 2004-2006 American Heart Association (AHA) Individual Postdoctoral Fellow 2002-2004 NIH NRSA Individual Postdoctoral Fellow 1996-2001 NSF Graduate Research Training Fellow

研究领域

Protein structure/function and dynamics; Electron and nuclear magnetic resonance spectroscopies; photosynthetic and respiratory bioenergetics; metalloenzyme structure function

In the Cooley lab, we loosely endeavor to understand how protein dynamics are involved in a lipid solubilized enzyme’s structure and function. There is a growing body of structural knowledge about this molecularly complex class of proteins, yet, the big black box lies in the understanding how protein dynamics influence catalysis or structural stability. This area of biophysical investigation of membrane-associated proteins currently lags significantly behind those of proteins belonging to more soluble classes of enzymes. Much of this lag has to do with the limited translation of common spectroscopic techniques (NMR, FRET, etc….) towards the investigation of these amphiphillic polypeptides. Therefore, a large focus of the lab is to develop spectroscopic methods that are more amenable to membrane associated analyses in the time domain. Our Lab is the first to employ to any significant extent deep-UV excited resonance Raman spectroscopy to monitor the structure and dynamics of membrane proteins. In doing so, we have identified a previously unknown sensitivity of this method for peptide backbone solvation allowing us to determine simultaneously peptide backbone structural fluctuations and their solvation (i.e. localizing changes to the membrane interior or exterior). By combining this promising technique with other methods such as EPR, CD, DLS, NMR, FRET and AFM to name just a few and combining methods with novel and classical strategies involving artificial lipid bilayer systems, we are currently interested in how folding, solvation and equilibration of proteins with various types of lipid bilayers influence global structure in the time domain. The often comically interdisciplinary nature of the lab leads to a robust training and education of all of the lab members from the many undergraduate researchers to the PhD students to myself the PI. To come join the fray and make a difference in all our lives contact me Cooleyjw@missouri.edu.

近期论文

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King J. D., Harrington L., Lada, B. M., He G., Cooley, J. W. and R. E. Blankenship. Site-directed mutagenesis of the highly perturbed copper site of auracyanin D. Archives in Biochemistry and Biophysics. 2014. In press. Miskowiec, A., Buck, Z. N., Brown, M. C., Kaiser, H., Hansen, F. Y. , King, G. M., Taub. H., Jiji, R., Cooley, J. W., Tyagi, M., Diallo, S. O., Mamontov, E., and K. W. Herwig. On the freezing behavior and diffusion of water in proximity to single supported zwitterionic and anionic bilayer lipid membranes. Europhysics Lett. 107: 28008. 2014. EPL Editors Choice Xiong, J., Roach, C. A., Oshokoya, O. O., Schroell, R. P., Yakubu, R. A., Eagleburger, M. K., Cooley, J. W. and R. D. JiJi. The Role of Bilayer Characteristics on the Structural Fate of Aß(1-40) and Aß(25-40). Biochemistry. 53:3004-11. 2014. Eagleburger, M. K., Cooley, J. W. and R. D. JiJi. Effects of fluidity on the ensemble structure of a membrane embedded a-helical peptide. Biopolymers. 101: 895-902. 2014. Brown, M. C., Yakubu, R. A., Taylor, J., Halsey, C. M., JiJi., R. D. and J. W. Cooley. Bilayer surface association of the pHLIP peptide promotes extensive backbone desolvation and helically-constrained structures. Biophysical Chemistry. 187: 1-6 . 2014. King J.D., McIntosh,C.L., Halsey,C.M., Lada,B.M., Cooley,J.W. and R.E.Blankenship. Metalloproteins diversified–The auracyanins are a family of cupredoxins which stretch the spectral and redox limits of blue copper proteins. Biochemistry. 52: 8267-8275. 2013. J. W. Cooley. Protein conformational changes involved in the cytochrome bc1 complex catalytic cycle. Biochimica et Biophysica Acta-Bioenergetics. 1827: 1340-1345. 2013. Brown, M. C., Mutter, A. C., Koder, R. L., JiJi, R. D. and J. W. Cooley. Observation of persistent a-helical content and discrete types of backbone disorder during a molten globule to ordered peptide transition via deep-UV resonance Raman spectroscopy. Journal of Raman Spectroscopy. 44(7):957–962. 2013. Mrutu, A., Lane, A. C., Drewett, J. M., Yourstone, S. D., Barnes, C. L., Halsey, C. M., Cooley, J. W. and J. R. Walensky. Molecular Structure and Spectroscopy of Diva- lent First Row Transition Metals, Mn-Zn, with Salicylaldiminate Ligands. Polyhedron, 54:300–308. 2013. Halsey, C. M., Benham, D., JiJi, R. D., and J. W. Cooley. Influence of the lipid environment on valinomycin structure and cation complex formation. Spectrochimica Acta Part A, 96:200–206, 2012. Halsey, C. M., Oshokoya, O. O., JiJi, R. D., and J. W. Cooley. Deep-UV Resonance Ra- man Analysis of the Rhodobacter capsulatus Cytochrome bc1 Complex Reveals a Potential Marker for the Transmembrane Peptide Backbone. Biochemistry, 50(30):6531– 6538, 2011. Biochemistry Editors Choice Halsey, C. M., Xiong, J., Oshokoya, O. O., Johnson, J. A., Shinde, S., Beatty, J. T., Ghirlanda, G., JiJi, R. D., and J. W. Cooley. Simultaneous Observation of Peptide Backbone Lipid Solvation and a- Helical Structure by Deep-UV Resonance Raman Spectroscopy. ChemBioChem, 12(14):2125–2128, 2011.