Virtual screening for lead discovery.
Tang Y.T. and Marshall G.R. (2011) “Virtual screening for lead discovery.” Methods Mol Biol. 2011;716:1-22. doi: 10.1007/978-1-61779-012-6_1. (Abstract)
Category: All Publications
Atomistic Folding Simulations of the Five-Helix Bundle Protein λ6−85
Bowman, G.R., Voelz, V.A. and Pande, V.S.
Atomistic Folding Simulations of the Five-Helix Bundle Protein λ6−85
J Am Chem Soc 133:664-667. (2011). (Abstract)
ROSETTA3: an object-oriented software suite for the simulation and design of macromolecules.
Leaver-Fay A., Tyka M., Lewis S.M., Lange O.F., Thompson J., Jacak R., Kaufman K., Renfrew P.D., Smith C.A., Sheffler W., Davis I.W., Cooper S., Treuille A., Mandell D.J., Richter F., Ban Y.E., Fleishman S.J., Corn J.E., Kim D.E., Lyskov S., Berrondo M., Mentzer S., Popović Z., Havranek J.J., Karanicolas J., Das R., Meiler J., Kortemme T., Gray J.J., Kuhlman B., Baker D., and Bradley P. (2011) “ROSETTA3: an object-oriented software suite for the simulation and design of macromolecules.” Methods Enzymol. 2011;487:545-74. doi: 10.1016/B978-0-12-381270-4.00019-6. (Abstract)
The role of Zn2+ on the structure and stability of murine adenosine deaminase.
Niu W., Shu, Q., Chen Z., Mathews F.S., Di Cera E., & Frieden C. (2010). “The role of Zn2+ on the structure and stability of murine adenosine deaminase.” J Phys Chem B. 2010 Dec 16;114(49):16156-65. doi: 10.1021/jp106041v. Epub 2010 Sep 3. (Abstract)
5′-Single-stranded/duplex DNA junctions are loading sites for E. coli UvrD translocase.
Tomko E.J., Jia H., Park J., Maluf N.K., Ha T., & Lohman T.M. (2010). “5′-Single-stranded/duplex DNA junctions are loading sites for E. coli UvrD translocase.” EMBO J. 2010 Nov 17;29(22):3826-39. doi: 10.1038/emboj.2010.242. Epub 2010 Sep 28. (Abstract)
SKATE: a docking program that decouples systematic sampling from scoring.
Feng J.A. and Marshall G.R. (2010) “SKATE: a docking program that decouples systematic sampling from scoring.” J Comput Chem. 2010 Nov 15;31(14):2540-54. doi: 10.1002/jcc.21545. (Abstract)
Taming the complexity of protein folding
Bowman, G.R., Voelz, V.A. and Pande, V.S.
Taming the complexity of protein folding
Curr Opin Struct Biol 21:4-11. (2011). (Abstract)
The association−dissociation behavior of the ApoE proteins: kinetic and equilibrium studies.
Garai K. & Frieden C. (2010). “The association−dissociation behavior of the ApoE proteins: kinetic and equilibrium studies.” Biochemistry. 2010 Nov 9;49(44):9533-41. doi: 10.1021/bi101407m. (Abstract)
An alternative pathway for Okazaki fragment processing: resolution of fold-back flaps by Pif1 helicase.
Pike, J.E., Henry, R.A., Burgers, P.M., Campbell, J.L. and Bambara, R.A.
An alternative pathway for Okazaki fragment processing: resolution of fold-back flaps by Pif1 helicase.
J Biol Chem 285:41712-41723 (2010). (Abstract)
Dry molten globule intermediates and the mechanism of protein unfolding.
Baldwin R.L., Frieden C., & Rose G.D. (2010). “Dry molten globule intermediates and the mechanism of protein unfolding.” Proteins. 2010 Oct;78(13):2725-37. doi: 10.1002/prot.22803. (Abstract)