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Home arrow People arrow Faculty Tuesday, 24 November 2009

DAVID A. JOHNSON, PH.D.

Professor of Biomedical Sciences
Ph.D., University of California, San Francisco, California

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Research Summary

Quantitative Fluorescence Spectroscopic Analysis of Protein Structure and Dynamics.

The central focus of the laboratory is toward the development and the use of primarily quantitative fluorescence spectroscopic methods to understand at a molecular level how drugs and proteins work. Systems studied include: the acetylcholine binding protein, cAMP-dependent protein kinase, acetylcholinesterase, and Pak2 kinase.

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Recent Publications
Tan, D., Johnson, D. A., Wu, W., Zeng, W., Chen, Y. H., Vonderhaar, B. K., & Walker, A. W. 2005 Prolactin (PRL) and S179D PRL-initiated Bioluminescence Resonance Energy Transfer Between Homo- and Hetero-pairs of Long and Short Human Prolactin Receptors in Living Human Cells. Molecular Endocrinology (in press).

Yang, S., Rogers, K. M., and Johnson, D. A. 2005 MgATP-induced conformational change of the catalytic subunit of cAMP-dependent protein kinase. Biophysical Chemistry 113, 93-99.

Boyd, A. E., Dunlop, C. S., Marnett, A. B., Wong, L., Taylor, P., and Johnson, D. A. 2004 Nanosecond Dynamics of the Mouse Acetylcholinesterase near the Active-Site Gorge, J. Biol. Chem. 279: 26612-26618.

Zawadzki, K. M., Chia-Pin Pan, C.-P., Johnson, D.A. Barkley, M.D., Taylor, S.S. 2003 Endogenous Tryptophan Residues of cAPK Regulatory Subunit Type IIβ Reveal Local Variations in Chemical Environments and Dynamic States, 2003 Proteins: Structure, Function and Genetics 51: 552-561.

Shi, J., Tai, K., McCammon, J.A., Taylor, P., and Johnson, D. A. 2003 Nanosecond Dynamics of the Mouse Acetylcholinesterase Cys69-Cys96 Omega Loop, 2003 J. Biol. Chem. 33: 30905-30911.

Li, F., Gangal, M., Juliano, C., Gorfain, E., Taylor, S.S. & Johnson, D.A. 2002. Evidence for an internal entropy contribution to phosphoryl transfer: a study of domain closure, backbone flexibility, and the catalytic cycle of cAMP-dependent protein kinase. J. Mol. Biol. 315: 459-469.

Johnson, D.A., Akamine, P., Radzio-Andzelm, E., Madhusudan, M. & Taylor S.S. 2001. Dynamics of cAMP-Dependent Protein Kinase. Chem. Rev. 101: 2243-2270.

Li, F., Gangal, M., Jones, J.M., Deich, J., Lovett, K.E., Taylor, S.S. & Johnson, D.A. 2000. Consequences of cAMP and Catalytic-Subunit Binding on the Flexibility of the A-Kinase Regulatory Subunit. Biochemistry 39: 15626-15632.

Garzon-Rodriguez, W., Vega, A., Sepulveda-Becerra, M., Milton, S., Johnson, D.A., Yatsmirsky, A.K. & Glabe, G. 2000. A Conformation Change in the Carboxyl-terminus of Alzheimer's Ab(1-40) Accompanies the Transition from Dimer to Fibril as Revealed by Fluorescence Quenching Analysis. J. Biol. Chem. 275: 22645-22649.

Gangal, M., Clifford, T., Deich, J., Cheng, X., Taylor, S.S. & Johnson, D.A. 1999. Mobilization of the A-Kinase through an Isoform-Specific Intermolecular Switch. PNAS 96, 12394-12399.

Johnson, D. A., Nguyen, B., Bohorquez, A. F., & Valenzuela, C. F. 1999. Paramagnetic Fluorescence Quenching in a Model Membrane: A Consideration of Lifetime and Temperature. Biophysical Chemistry, 77, 1-9.

Hauer, J. A. Taylor, S. S., & Johnson, D.A. 1999. Binding-Dependent Disorder-Order Transition in PKI-alpha: A Fluorescence Anisotropy Study. Biochemistry, 38, 6774-6780.

Gangal, M., Cox, S., Lew, J., Clifford, T., Garrod, S. M., Aschbaher, M.,Taylor, S. S., and Johnson, D. A. 1998. Backbone Flexibility of Five Sites on the Catalytic Subunit of cAMP-Dependent Protein Kinase in the Open and Closed Conformations. Biochemistry 37, 13728-13735.

Johnson, D. A. and Ayres, S. 1996. Quinacrine noncompetitive inhibitor binding site localized on the nicotinic acetylcholine receptor in the open state. Biochemistry 35, 6330-6336.

Yang, S., Fletcher, W. H., and Johnson, D. A., 1995. Regulation of cAMP-dependent protein kinase: Enzyme activation without dissociation. Biochemistry 34, 6267-6271.

Johnson, D.A. and Nuss, J., 1994. The phencyclidine-sensitive ethidium binding site is located outside the transmembrane domain of the nicotinic acetylcholine receptor: a fluorescence study. Biochemistry 33, 9070-9077.

Valenzuela, C. F., Dowling, A. J., Arias, H.R., and Johnson, D.A., 1994. Antibody-induced conformational changes in the Torpedo acetylcholine receptor: a fluorescence study. Biochemistry 33, 6586-6594.

Valenzuela, C. F., Wiegn, P., Yguerabide, J., and Johnson, D.A. 1994. Transverse distance between the agonist binding sites and the membrane on the Torpedo acetylcholine receptor: a fluorescence study. Biophys. J. 66, 674-682.
 

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