More recent publications (2000-present)

Techniques and miscellaneous

  • P. Kollman, I. Massova, C. Reyes, B. Kuhn, S. Huo, L. Chong, M. Lee, T. Lee, Y. Duan, W. Wang, O. Donini, P. Cieplak, J. Srinivasan, D.A. Case and T.E. Cheatham, III. Calculating structures and free energies of complex molecules: Combining molecular mechanics and continuum models. Accts. Chem. Res. 33, 889-897 (2000).

  • P.F. Batcho, D.A. Case, and T. Schlick. Optimized particle-mesh Ewald/multiple-timestep integration for molecular dynamics simulations J. Chem. Phys. 115, 4003-4018 (2001).

  • P.A. Kollman and D.A. Case. Drug-target binding forces: Advances in force field approaches. Burger's Medicinal Chemistry, Sixth Edition. Vol. 1: Drug Discovery. D.J. Abraham, Ed. (New York, John Wiley & Sons, 2003), pp. 169-185.

  • D. A. Case and D. R. Herschbach. Statistical theory of angular momentum polarization in chemical reactions. Mol. Phys. 100, 109-125 (2002). [This is a reprinted version of a 1975 paper, chosen as one of the most significant papers of the first 100 issues of Molecular Physics. See also the commentary by D.C. Cleary: Mol. Phys. 100, 107 (2002).]

  • H. Liu, C. Qu, J.E. Johnson and D.A. Case. Pseudo-atomic models of swollen CCMV from cryo-electron micrscopy data. J. Struct. Biol. 142, 356-363 (2003).

  • J.W. Ponder and D.A. Case. Force fields for protein simulations. Adv. Prot. Chem. 66, 27-85 (2003). (Illustration shows a solvated free energy surface for the alanine dipeptide.)

  • J. Wang, R.M. Wolf, J.W. Caldwell, P.A. Kollman and D.A. Case. Development and testing of a general Amber force field. J. Comput. Chem. 25, 1157-1174 (2004).

  • D.A. Case, T.E. Cheatham, III, T. Darden, H. Gohlke, R. Luo, K.M. Merz, Jr., A. Onufriev, C. Simmerling, B. Wang and R. Woods. The Amber biomolecular simulation programs. J. Computat. Chem. 26, 1668-1688 (2005).

  • J. Wang, W. Wang, P.A. Kollman and D.A. Case. Automatic atom type and bond type perception in molecular mechanical calculations. J. Mol. Graphics. Model. 25, 247-260 (2006).

  • F. Paesani, W. Zhang, D.A. Case, T.E. Cheatham III, and G.A. Voth. An accurate and simple quantum model for liquid water. J. Chem. Phys. 125, 184507 (2006).

  • G.M. Seabra, R.C. Walker, M. Elstner, D.A. Case, and A.E. Roitberg. Implementation of the SCC-DFTB method for hybrid QM/MM simulations within the Amber molecular dynamics package. J. Phys. Chem. A 111, 5655-5664 (2007).

  • R.C. Walker, M.F. Crowley and D.A. Case. The implementation of a fast and accurate QM/MM potential method in Amber. J. Comput. Chem. 28, 1019-1031 (2008).

  • T. Steinbrecher, D.L. Mobley and D.A. Case. Non-linear scaling schemes for Lennard-Jones interactions in free energy calculations. J. Chem. Phys. 127, 214018 (2007).

    Electrostatic interactions in biomolecules

  • D. Bashford and D.A. Case. Generalized Born models of macromolecular solvation effects. Annu. Rev. Phys. Chem. 51, 129-152 (2000).

  • A. Onufriev, D. Bashford and D.A. Case. A modification of the generalized Born model suitable for macromolecules. J. Phys. Chem. 104, 3712-3720 (2000).

  • V. Tsui and D.A. Case. Molecular dynamics simulations of nucleic acids using a generalized Born solvation model. J. Am. Chem. Soc. 122, 2489-2498 (2000).

  • A. Onufriev, D.A. Case and G.M. Ullmann. A novel view of pH titration in biomolecules. Biochemistry 40, 3413-3419 (2001).

  • C.P. Sosa, T. Hewitt, M.S. Lee and D.A. Case. Vectorization of the generalized Born model for molecular dynamics on shared-memory computers. J. Mol. Struct. (Theochem) 549, 193-201 (2001).

  • V. Tsui and D.A. Case. Theory and applications of the generalized Born solvation model in macromolecular simulations. Biopolymers: Nucleic Acid Sciences 56, 275-291 (2001).

  • A. Onufriev, D.A. Case and D. Bashford. Effective Born radii in the generalized Born approximation: The importance of being perfect. J. Computat. Chem. 23, 1297-1304 (2002).

  • M. Feig, A. Onufriev, M.S. Lee, W. Im, D.A. Case and C.L. Brooks, III. Performance comparison of generalized Born and Poisson methods in the calculation of electrostatic solvation energies for protein structures. J. Comput. Chem. 25, 265-284 (2004).

  • A. Onufriev, D. Bashford and D.A. Case. Exploring protein native states and large-scale conformational changes with a modified generalized Born model. Proteins 55, 383-394 (2004).

  • T. Simonson, J. Carlsson and D.A. Case. Proton binding to proteins: pKa calculations with explicit and implicit solvent models. J. Am. Chem. Soc. 126, 4167-4180 (2004).

  • V. Roberts, D.A. Case, and V. Tsui. Predicting interactions of winged-helix transcription factors with DNA. Proteins 57, 172-87 (2004). (Illustration at right shows the protein/DNA binding motif)

  • J. Mongan, D.A. Case and J.A. McCammon. Constant pH molecular dynamics in generalized Born implicit solvent. J. Comput. Chem. 25, 2038-2048 (2004).

  • J. Mongan and D.A. Case. Biomolecular simulations at constant pH. Curr. Opin. Struct. Biol. 15, 157-163 (2005).

  • R.C. Rizzo, T. Aynechi, D.A. Case and I.D. Kuntz. Estimation of absolute free energies of hydration using continuum methods: Accuracy of partial charge models and optimization of nonpolar contributions. J. Chem. Theory Comput. 2, 128-139 (2006).

  • N.A. Baker, D. Bashford and D.A. Case. Implicit solvent electrostatics in biomolecular simulation. In New Algorithms for Macromolecular Simulation, B. Leimkuhler, C. Chipot, R. Elber, A. Laaksonen, A. Mark, T. Schlick, C. Schütte, and R. Skeel, eds. (New York: Springer-Verlag, 2006), pp. 263-295.

  • R.A. Brown and D.A. Case. Second derivatives in generalized Born theory. J. Comput. Chem. 27, 1662-1675 (2006).

  • J. Mongan, C. Simmerling, J.A. McCammon, D.A. Case, and A. Onufriev. Generalized Born model with a simple, robust molecular volume correction. J. Chem. Theory Comput. 3, 156-169 (2007).

    Dynamics of peptides and proteins

  • W. Cornell, R. Abseher, M. Nilges and D.A. Case. Continuum solvent molecular dynamics study of flexibility in interleukin-8. J. Mol. Graphics Model. 19, 136-145 (2001).

  • R. Jimenez, D.A. Case and F.E. Romesberg. Flexibility of an antibody binding site measured with photon echo spectroscopy. J. Phys. Chem. B106, 1090-1103 (2002).

  • A. Onufriev, D.A. Case and D. Bashford. Structural details, pathways, and energetics of unfolding of apomyoglobin. J. Mol. Biol. 325, 555-567 (2003).

  • H. Gohlke, C. Kiel, and D.A. Case. Insights into protein-protein binding by binding free energy calculation and free energy decomposition for the Ras-Raf and Ras-RalGDS complexes. J. Mol. Biol. 330, 891-913 (2003).

  • H. Gohlke, L. Kuhn and D.A. Case. Change in flexibility upon complex formation: Analysis of Ras-Raf using molecular dynamics and a molecular framework approach. Proteins 56, 322-337 (2004). (Illustration shows the graph model used in the FIRST molecular framework approach)

  • H. Gohlke and D.A. Case. Converging free energy estimates: MM-PB(GB)SA studies on the protein-protein complex Ras-Raf. J. Comput. Chem. 25, 238-250 (2004).

  • T. Steinbrecher, D.A. Case and A. Labahn. A multistep approach to structure based drug design: Studying ligand binding at the human neutrophil elastase. J. Med. Chem. 49, 1837-1844 (2006).

  • R.J. Payne, S. Ficht, S. Tang, A. Brik, Y.-Y. Yang, D.A. Case and C.-H Wong. Extended sugar-assisted glycopeptide ligations: Development, scope and application. J. Am. Chem. Soc. 129, 13527-13536 (2007).

  • F.Y. Dupradeau, S. Pissard, M.P. Coulhon, E. Cadet, K. Foulon, C. Fourcade, M. Goossens, D.A. Case, and J. Rochette. An unusual compound heterozygosity in HFE Hemochromatosis (p.G43D-H63D/p.C282Y): a computationally-based study of the cis mutations with implication in binding to transferrin receptor 1. Human Mutation 29, 206 (2008).

  • A.P. Graves, D.M. Shivakumar, S.E. Boyce, M.P. Jacobson, D.A. Case and B. Shoichet. Rescoring docking hit lists for model cavity sites: predictions and experimental testing. J. Mol. Biol. 377, 914-934 (2008).

  • T. Hou, W. Zhang, D.A. Case, and W. Wang. Deciphering the binding patterns of the peptide ligands of amphiphysin-1 SH3 domain by analyzing the molecular interaction fields. J. Mol. Biol. (in press).

    DNA/RNA Secondary and Tertiary Structure

  • A.K. Ogawa, O.K. Abou-Zied, V. Tsui, R. Jimenez, D.A. Case and F.E. Romesberg. A photo-tautomerizable model DNA base pair. J. Am. Chem. Soc. 122, 9917-9920 (2000).

  • M.S. VanLoock, A. Malhotra, D.A. Case, R. Agrawal, P. Penczek, T.R. Easterwood, J. Frank and S.C. Harvey, "A functional interpretation of the cryo-electron microscopy map of the 30S ribosomal subunit from Escherichia coli. In The Ribosome: Structure, Function, Antibiotics and Cellular Interactions, R.A. Garrett, S.R. Douthwaite, A. Liljas, A.T. Matheson, P.B. Moore and H.F. Noller, eds. (Washington, DC: ASM Press, 2000), pp. 165-171.

  • V. Tsui and D.A. Case. Calculations of the absolute free energies of binding between RNA and metal ions using molecular dynamics simulations and continuum electrostatics. J. Phys. Chem. B 105, 11314-11325 (2001).

  • T. Macke, D. Ecker, R. Gutell, D. Gautheret, D.A. Case and R. Sampath. RNAMotif: A new RNA secondary structure definition and discovery algorithm. Nucl. Acids Res. 29, 4724-4735 (2001).

  • A. Waugh, P. Gendron, R. Altman, J.W. Brown, D. Case, D. Gautheret, S.C. Harvey, N. Leontis, J. Westbrook, E. Westhof, M. Zuker and F. Major. RNAML: A standard syntax for exchanging RNA information. RNA 8, 707-717 (2002).

  • H. Gouda, I.D. Kuntz, D.A. Case and P.A. Kollman. Free energy calculations for theophylline binding to an RNA aptamer: Comparison of MM-PBSA and thermodynamic integration methods. Biopolymers 68, 16-34 (2003).

  • V. Tsui, T. Macke, and D.A. Case. A novel method for finding tRNA genes. RNA 9, 507-517 (2003). (Figure shows a "descriptor" for finding tRNA genes in prokaryotes.)

  • H.T. Allawi, M.W. Kaiser, A.V. Onufriev, W.-P. Ma, A.E. Brogard, D.A. Case, B.P. Neri and V.I Lyamichev. Modeling of flap endonuclease interactions with DNA substrate. J. Mol. Biol. 328, 537-554 (2003).

  • D.L. Beveridge, G. Barreiro, S. Byun, D.A. Case, T.E. Cheatham, III, S.B. Dixit, E. Giudice, F. Lankas, R. Lavery, J. Maddocks, R. Osman, H. Sklenar, G. Stoll, K.M. Thayer, P. Varnai and M.A. Young. Molecular dynamics simulations of the 136 tetranucleotide sequences of DNA oligonucleotides. I. Research design, informatics, and results on d(CpG) steps. Biophys. J. 87, 3799-3813 (2004).

  • S.B. Dixit, D.L. Beveridge, D.A. Case, T.E. Cheatham, III, E. Giudice, F. Lankas, R. Lavery, J.H. Maddocks, R. Osman, H. Sklenar, K.M. Thayer, and P. Varnai. Molecular dynamics simulations of the 136 unique tetranucleotide sequences of DNA oligonucleotides. II. Sequence context effects on the dynamical structures of the 10 unique dinucleotide steps. Biophys. J. 89, 3721-3740 (2005).

  • F.-Y. Dupradeau, D.A. Case, C. Yu, R. Jimenez and F.E. Romesberg. Differential solvation and tautomer stability of a model base pair withing the minor and major groove of DNA. J. Am. Chem. Soc. 127, 15612-15617 (2005).

  • T.E. Cheatham, III and D.A. Case. Using Amber to simulate DNA and RNA. In Computational Studies of DNA and RNA, J. Sponer and F. Lankas, eds. (Dordrecht: Springer, 2006), pp 45-72.

  • D.H. Mathews and D.A. Case. Nudged Elastic Band calculation of minimal energy pathways for the conformational change of a GG mismatch. J. Mol. Biol. 357, 275-291 (2006).

  • Q. Cui, R.K.-Z. Tan, S.C. Harvey and D.A. Case. Low-resolution molecular dynamics simulations of the 30S ribosomal subunit. Multiscale Model. Simul. 5, 1248-1263 (2006).

  • R.K. Grover, S.J. Pond, Q. Cui, P. Subramaniam, M. Puga, D.A. Case, D.P. Millar and P. Wentworth, Jr. O-Glycoside orientation is an essential aspect of base J recognition by the kinetoplastid DNA-binding protein JBP1. Angew. Chemie 46, 2839-2843 (2007).

    Active sites of iron-sulfur (and related) proteins

  • D.A. Case, L. Noodleman and J. Li. Modern computational approaches to modeling polynuclear transition metal complexes. In Metal-Ligand Interactions in Physics, Chemistry and Biology, N. Russo and D.R. Salahub, eds. (Dordrecht: Kluwer, 2000), pp. 19-47.

  • T. Lovell, J. Li, T. Liu, D.A. Case and L. Noodleman. FeMo cofactor of nitrogenase: A density functional study of states MN, MOX, MR and MI. J. Am. Chem. Soc. 123, 12392-12410 (2001).

  • G.M. Ullmann, L. Noodleman and D.A. Case. Density functional calculation of the pKa values and redox potentials in the bovine Rieske iron-sulfur protein. J. Biol. Inorg. Chem. 7, 623-639 (2002).

  • T. Lovell, J. Li, D.A. Case and L. Noodleman. FeMo cofactor of nitrogenase: Energetics and local interactions in the protein environment. J. Biol. Inorg. Chem. 7, 735-749 (2002).

  • T. Lovell, J. Li, D.A. Case and L. Noodleman. Binding modes for the first coupled electron and proton addition to FeMoco of nitrogenase. J. Am. Chem. Soc. 124, 4546-4547 (2002).

  • T. Lovell, R.A. Torres, W.-G. Han, T. Liu, D.A. Case and L. Noodleman. Metal substitution in the active site of nitrogenase MFe7S9 (M=Mo4+, V3+, Fe3+. Inorg. Chem 41, 5744-5753 (2002).

  • R.A. Torres, T. Lovell, L. Noodleman and D.A. Case. Density functional and reduction potential calculations of Fe4S4 clusters. J. Am. Chem. Soc. 125, 1923-1936 (2003).

  • J.A. Fee, J.M. Catagnetto, D.A. Case, L. Noodleman, C.D. Stout and R.A. Torres. The circumsphere as a tool to assess distortion in [4Fe-4S] atom clusters. J. Biol. Inorg. Chem. 8, 519-526 (2003). (Figure shows a geometric analysis of these cubane systems.)

  • R.-J. Cheng, P.-Y. Chen, T. Lovell, T. Liu, L. Noodleman and D.A. Case. Symmetry and bonding in metalloporphyrins. A modern implementation for the bonding analyses of five- and six-coordinate high-spin iron(III) porphyrin complexes through density functional calculation and NMR spectroscopy. J. Am. Chem. Soc. 125, 6774-6783 (2003).

  • Y. Xiao, M. Koutmos, D.A. Case, D. Coucouvanis, H. Wang and S.P. Cramer. Dynamics of an [Fe4S4(SPh)4]2- cluster via IR, Raman, and nuclear resonant vibrational spectroscopy (NRVS). Analysis using 36S substitution, DFT and empirical force fields. J. Chem. Soc. Dalton, 2192-2201 (2006).

  • Y. Xiao, K. Fisher, M.C. Smith, W.E. Newton, D.A. Case, S.J. George, H. Wang, W. Sturhahn, E.E. Alp, J. Zhao, Y. Yoda and S.P. Cramer. How nitrogenase shakes--initial information about P-cluster and FeMo-cofactor normal modes from nuclear resonance vibrational spectroscopy (NRVS). J. Am. Chem. Soc. 128, 7608-7612 (2006).

  • D. Lukoyanov, V. Pelmenschikov, N. Maeser, M. Laryukhin, T.C. Yang, L. Noodleman, D.R. Dean, D.A. Case, L.C. Seefeldt, and B.M. Hoffman. Testing if the interstitial atom, X, of the nitrogenase molybdenum-iron cofactor is N or C: ENDOR, ESEEM, and DFT Studies of the S = 3/2 resting state in multiple environments. Inorg. Chem. 46, 11437-11439 (2007).

  • Y. Guo, H. Wang, Y. Xiao, S. Vogt, R.K. Thauer, S. Shima, P.I. Volkers, T.B. Rauchfuss, V. Pelmentschikov, D.A. Case, E.E. Alp, W. Sturhahn, Y. Yoda, and S.P. Cramer. Characterization of the Fe Site in Methanothermobacter marburgensis Hydrogenase (mHmd) and a Model Compound via Nuclear Resonance Vibrational Spectroscopy (NRVS). Inorg. Chem. (in press).

    Analysis of chemical shifts in proteins and nucleic acids

  • D.S. Wishart and D.A. Case. Use of chemical shifts in macromolecular structure determination. Meth. Enzymol. 338, 3-34 (2001).

  • X.P. Xu and D.A. Case. Automated prediction of 15N, 13C`alpha`, 13C`beta` and 13C' chemical shifts in proteins using a density functional database. J. Biomol. NMR 21 321-333 (2001).

  • X.P. Xu and D.A. Case. Probing multiple effects on 15N, 13C`alpha`, 13C`beta` and 13C' chemical shifts in peptides using density functional theory. Biopolymers 65, 408-423 (2002). (Figure shows some effects of hydrogen bonds on heavy atoms shifts in peptides)

  • S. Moon and D.A. Case. A comparison of quantum chemical models for calculating NMR shielding parameters in peptides : Mixed-basis-set and ONIOM methods combined with a complete basis-set extrapolation. J. Comput. Chem. 27, 825-836 (2006).

  • S. Moon and D.A. Case. A new model for chemical shifts of amide hydrogens in proteins. J. Biomol. NMR 138, 139-150 (2007).

  • S. Tang and D.A. Case. Vibrational averaging of chemical shift anisotropies in model peptides. J. Biomol. NMR. 38, 255-266 (2007).

    Analysis of spin-spin coupling constants

  • V. Tsui, L. Zhu, T.-H. Huang, P.E. Wright and D.A. Case. Assessment of zinc finger orientations by residual dipolar coupling constants. J. Biomol. NMR 16, 9-21 (2000).

  • D.A. Case. Interpretation of chemical shifts and coupling constants in macromolecules. Curr. Opin. Struct. Biol. 10, 197-203 (2000).

  • G. Cornilescu, A. Bax and D.A. Case. Large variations in one-bond 13C`alpha`-13C`beta` J couplings in polypeptides correlate with backbone conformation. J. Am. Chem. Soc. 122, 2168-2171 (2000).

  • D.A. Case, C. Scheurer and R. Brüschweiler. Density functional calculations of scalar 3J couplings in peptides and proteins. J. Am. Chem. Soc. 122, 10390-10397 (2000).

  • J.J. Chou, D. Case and A. Bax. Insights in mobility of methyl-bearing sidechains in proteins from 3JCC and 3JCN couplings. J. Am. Chem. Soc. 125, 8959-8966 (2003).

    Structure and dynamic analysis using NMR or X-ray data -- methods

  • D.A. Case. Molecular dynamics and NMR spin relaxation in proteins. Acc. Chem. Res. 35, 325-331 (2002).

  • B. Xia, V. Tsui, D.A. Case, H.J. Dyson and P.E. Wright. Comparison of protein solution structures refined in vacuum, with a generalized Born model, and with explicit water. J. Biomol. NMR 22, 317-331 (2002).

  • L. Moulinier, D.A. Case and T. Simonson. Re-introducing electrostatics into protein X-ray structure refinement: bulk solvent treated as a dielectric continuum. Acta Cryst. D 59, 2094-2103 (2003). (Figure shows a piece of X-ray density using an implicit solvent refinement model.)

  • M.F. Roberts, Q. Cui, C.J. Turner, D.A. Case and A.G. Redfield. High resolution field-cycling NMR studies of a DNA octamer as a probe of phosphodiester dynamics, and comparisons with computer simulation. Biochemistry 43, 3637-3650 (2004).

  • V. Wong and D.A. Case. Evaluating rotational diffusion from protein MD simulations. J. Phys. Chem. B, (in press, asap).

    Structure refinement using NMR data -- structures

  • G.B. Legge, R.W. Kriwacki, J. Chung, U. Hommel, P. Ramage, D.A. Case, H.J. Dyson and P.E. Wright. NMR solution structure of the inserted domain of human leukocyte function associated antigen-1. J. Mol. Biol. 295, 1251-1264 (2000).

  • J.A. Smith, G. Bifulco, D.A. Case, D.L. Boger, L. Gomez-Paloma and W.J. Chazin. The structural basis for in situ activation of DNA alkylation by duocarmycin SA. J. Mol. Biol. 300, 1195-1204 (2000).

  • V. Tsui, I. Radhakrishnan, P.E. Wright and D.A. Case. NMR and molecular dynamics studies of the hydration of a zinc finger-DNA complex. J. Mol. Biol. 302, 1101-1117 (2000).

  • M.V. Botuyan, G. Mer, G.-S. Yi, C.M. Koth, D.A. Case, A.M. Edwards, W.J. Chazin and C.H. Arrowsmith. Solution structure and dynamics of yeast elongin C in complex with a von Hippel-Lindau peptide. J. Mol. Biol. 312, 177-186 (2001).

  • Q. Zhang, T. Dwyer, V. Tsui, D. Case, J. Cho, P.B. Dervan and D.E. Wemmer. NMR structure of a cyclic polyamide-DNA complex. J. Am. Chem. Soc. 126, 7958-7966 (2004). (Figure shows a superposition of NMR structures for this complex.)

  • B.M. Lee, J. Xu, B.K. Clarkson, M.A. Martinez-Yamout, H.J. Dyson, D.A. Case, J.M. Gottesfeld, and P.E. Wright. Induced fit and "lock and key" recognition of 5S RNA by zinc fingers of transcription factor IIIA. J. Mol. Biol. 357, 275-291 (2006).

  • J. Chen, F.-Y. Dupradeau, D.A. Case, C.J. Turner and J. Stubbe. NMR structural studies and molecular modeling of duplex DNA containing normal and 4'-oxidized abasic sites. Biochemistry 46, 3096-3107 (2007).

  • 221. J. Chen, F.-Y. Dupradeau, D.A. Case, C.J. Turner and J. Stubbe. DNA oligonucleotides with A, T, G, or C opposite an abasic site: Structure and dynamics. Nucl. Acid Res. 36, 253-262 (2008).



    Updated on April 17, 2008. Comments to case@scripps.edu