Douglas D. Root

Associate Professor

940-565-2683

www.biol.unt.edu/~droot/Index.html

BS, University of California at Irvine

PhD, Univesity of California at Los Angeles

Research

My laboratory's research on actin and actin-binding proteins uses sophisticated microscopic, spectroscopic, computational, and biochemical techniques to investigate their structure and function. Chemical attachments of the probes to specific sites on actin and myosin are characterized using single molecule assays, molecular mechanics, FPLC, electrophoretic, western blotting, ultracentrifugation, and enzymatic analyses. Nanoscale measurements of resonance energy transfer during the contractile process, enable analysis of atomic models.

Professional Experience

2002-present Associate Professor of Biological Sciences, UNT

1996-2002 Assistant Professor of Biological Sciences, UNT

1992-1996 Research Fellow, UT Austin

1987-1992 Tumor Cell Biology Predoctoral Fellow, UCLA

Awards and Honors

Grant awards: National Institute of Arthritis and Musculoskeletal Diseases, NIH;

National Institute of General Medical Sciences, NIH; American Heart Association Texas Affiliate.

Muscular Dystrophy Association Fellowship. NCI Tumor Cell Biology Predoctoral Fellowship.

Representative Publications

Zhang, Z., Jin, J.-P., and Root, D. D. (2004) "Binding of Calcium Ions to an Avian flight Muscle Troponin T," Biochemistry 43, 2645-2655.

Root, D. D., Vaccaro, C., Zhang, Z., and Castro, M. (2004) “Detection of Single Nucleotide Variations by a Hybridization Proximity Assay Based on Molecular Beacons and Luminescence Resonance Energy Transfer.” Biopolymers 75, 60-70.

Root, D. D. (2002) “The Dance of Actin and Myosin: A Review of the Mechanism of Actomyosin Motility.” Cell Biochem. Biophys. 37, 111-139.

Root, D. D. (2002) “A Computational Comparison of the Atomic Models of the Actomyosin Interface” Cell Biochem. Biophys. In Press.

Root, D. D., Stewart, S., and Xu, J. (2002) “Dynamic Docking of Myosin and Actin Observed with Resonance Energy Transfer.” Biochemistry 41, 1786-1794.

Root, D. D., and Wang, K. (2001) "High-Affinity Actin-Binding Nebulin Fragments Influence the ActoS1 Complex," Biochemistry 40, 1171-1186.

Xu, J., and Root, D. D. (2000) "Conformational Selection During Weak Binding at the Actin and Myosin Interface," Biophys. J. 79, 1498-1510.

Jin, J.-P., and Root, D. D. (2000) "Modulation of Troponin T Molecular Conformation and Flexibility by Metal Ion Binding to the NH 2 -Terminal Variable Region," Biochemistry 39, 11702-11713.

Teal, H. E., Hu, Z., and Root, D. D. (2000) "Native Purification of Biomolecules with Temperature-Mediated Hydrophobic Modulation Liquid Chromatography," Anal. Biochem. 283, 159-165.

Root, D. D., Shangguan, X., Xu, J., and McAllister, M. (1999) " Determination of Fluorescent Probe Orientations on Biomolecules by Conformational Searching: Algorithm Testing and Applications to the Atomic Model of Myosin," J. Struct. Biol. 127, 22-34. (+ Cover Photo)

Xu, J., and Root, D. D. (1998) "Domain Motion between the Regulatory Light Chain and the Nucleotide Site in Skeletal Muscle Myosin," J. Struct. Biol. 123, 150-161.

Root, D. D. (1997) " In Situ Molecular Association of Dystrophin with Actin Revealed by Sensitized Emission Immuno-Resonance Energy Transfer," Proc. Natl. Acad. Sci., USA , 94, 5685-5690.

Root, D. D., and Wang, K. (1996) "Copper Iodide Staining of Proteins on Solid Phases," In Protein Protocols Handbook (Ed. James Walker), Humana Press, Totowa, NJ, pp. 39-43.

Root, D. D., and Wang, K. (1994) "Calmodulin-Sensitive Interaction of Human Nebulin Fragments With Actin And Myosin," Biochemistry 33 , 12581-12591.

Cook, R. K., Root, D. D., Miller, C., Reisler, E., and Rubinstein, P. A. (1992) "Enhanced Stimulation of Myosin Subfragment 1 ATPase Activity by Addition of Negatively Charged Residues to the Yeast Actin N-Terminus." J. Biol. Chem. 268, 2410-2415.

Root, D. D., and Reisler, E. (1992) "Cooperativity of Thiol-Modified Myosin Filaments: ATPase and Motility Assays of Myosin Function," Biophysical Journal . 63, 730-740.