Green, David - Stony Brook University - Department of Chemistry

研究领域

Current research in the Green Lab is focused on two primary biological systems: (1) signal transduction through the heterotrimeric G-protein pathway; and (2) the initial steps in the recognition of target cells by the HIV-1 virus. Each of these systems is being used to explore two distinct general problems of biological interest. The G-protein signal transduction pathway is our focus for explorations of the specificity of protein–protein interactions, while HIV–cell recognition is our prototypical system for understanding the role of glycosylation in modulating the interactions of proteins. In each system, sub-projects are focused on specific questions.

近期论文

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D. F. Green. "A statistical framework for hierarchical methods in molecular simulation and design." J. Chem Theory Comput. In press (2010). N. Carrascal and D. F. Green. "Energetic decomposition with Generalized-Born and Poisson--Boltzmann solvent models: Lessons from association of G-protein components." J. Phys. Chem. B In press, available online. (2010). doi:10.1021/jp910540z H. Taskent-Sezgin, J. Chung, V. Patsalo, S. J. Miyake-Stoner, A. M. Miller, S. H. Brewer, R. A. Mehl, D. F. Green, D. P. Raleigh and I. Carrico "Interpretation of p-cyanophenylalanine fluorescence in proteins in terms of solvent exposure and contribution of side-chain quenchers: A combined fluorescence, IR and molecular dynamics study." Biochemistry 48 (38): 9040-9046 (2009). doi:10.1021/bi900938z Y. K. Fujimoto, R. N. TerBush and D. F. Green. "Computational models explain the oligosaccharide specificity of cyanovirin-N." Protein Science. 17 (11): 2008-2014 (2008). doi:10.1110/ps.034637.108 D. F. Green. "Optimized radii for continuum solvation calculations with carbohydrates." J. Phys. Chem. B 112 (16): 5238-5249 (2008). doi:10.1021/jp079725b D. F. Green, A. T. Dennis, P. S. Fam, B. Tidor and A. Jasanoff. "Rational design of new binding specificity by simultaneous mutagenesis of calmodulin and a target peptide." Biochemistry 45 (41): 12547-12557 (2006). doi:10.1021/bi060857u D. F. Green and B. Tidor. "Design of improved protein inhibitors of HIV-1 cell entry: Optimization of electrostatic interactions at the binding interface." Proteins: Struct. Func. Bioinf. 60 (4):644-657 (2005). doi:10.1002/prot.20540 B. A. Joughin, D. F. Green and B. Tidor. "Action-at-a-distance interactions enhance protein binding affinity." Protein Sci. 14 (5): 1363-1369 (2005). doi:10.1110/ps.041283105 D. F. Green and B. Tidor. "Eschericia coli glutaminyl-tRNA synthetase is electrostatically optimized for binding of its cognate substrates." J. Mol. Biol. 342 (2): 435-452 (2004). doi:10.1016/j.jmb.2004.06.087 C. Mattos, J. D. Cohen, D. F. Green, B. Tidor and M. Karplus. "X-ray structural and simulation analysis of a protein mutant: The value of a combined approach." Proteins: Struct. Func. Bioinf. 55 (3): 733-742 (2004). doi:10.1002/prot.20031 D. F. Green and B. Tidor. "A comprehensive evaluation of ab initio charge determination methods for use in continuum electrostatic calculations." J. Phys. Chem. B 107 (37): 10261-10273 (2003). doi:10.1021/jp0350971 F. Jiang, H. A. Jenkins, D. F. Green, G. P. A. Yap and R. K. Pomeroy. "A novel metal-chain extension reaction: synthesis of (X)[Os(CO)3(CNBut)]nMn(CO)5 (X = Cl, Br, I; n = 1, 2, 3)." Can. J. Chem 80 (3): 281-291 (2002). doi:10.1139/v02-016 R. J. Batchelor, D. F. Green, B. D. Johnston, B. O. Patrick and B. M. Pinto. "Conformational preferences in glycosylamines. Implications for the exo-anomeric effect." Carbohyd. Res. 330 (3): 421-426 (2001). doi:10.1016/S0008-6215(00)00304-9 K. D. Randell, B. D. Johnston, D. F. Green and B. M. Pinto. "Is there a generalized reverse anomeric effect? Substituent and solvent effects on the configurational equilibria of neutral and protonated N-arylglucopyranosylamines and N-aryl-5-thioglucopyranosylamines." J. Org. Chem 65 (1): 220-226 (2000). doi:10.1021/jo991520j