{"id":164,"date":"2018-02-06T14:39:36","date_gmt":"2018-02-06T19:39:36","guid":{"rendered":"https:\/\/sites.bu.edu\/cui-group\/?page_id=164"},"modified":"2018-02-06T14:39:47","modified_gmt":"2018-02-06T19:39:47","slug":"postdoc","status":"publish","type":"page","link":"https:\/\/sites.bu.edu\/cui-group\/papers\/postdoc\/","title":{"rendered":"QC Postdoc Years (1998-2001)"},"content":{"rendered":"

<\/a>39. Is “proton wire” concerted or step-wise? A model study of proton transfers in carbonic anhydrase, Q. Cui, M. Karplus, J. Phys. Chem. B 107, 1071-1078 (2003)\u00a0<\/span><\/span>PDF version<\/a><\/span><\/p>\n

<\/a>38. Understanding the role of active-site residues in chorimsmate mutase catalysis from molecular dynamics simulations, H. Guo, Q. Cui, W. N. Lipscomb, M. Karplus, Angew. Chim. Intl. Ed. 42, 1508-1511 (2003)<\/p>\n

<\/a>37. Does Chorismate Mutase catalyze a conformational change of the substrate prior to the chemical rearrangement? H. Guo, Q. Cui, W. N. Lipscomb, M. Karplus, NATO Sci. Ser. I 364, 63-74 (2005)<\/p>\n

<\/a>36. Modeling zinc in biomolecules with the Self-Consistent Charge Density Functional Tight-Binding (SCC-DFTB) method: application to structural and energetical analysis, M. Elstner, Q. Cui, P. Munih, E. Kaxiras, T. Frauenheim, and M. Karplus, J. Comput. Chem. 24, 565-581 (2003)\u00a0<\/span>PDF version<\/a><\/p>\n

<\/a>35. Combining ab initio and density functional theory with semi-empirical methods , Q. Cui, H. Guo, M. Karplus, J. Chem. Phys. 117, 5617-5631 (2002)\u00a0<\/span>PDF version<\/a><\/p>\n

<\/a>34. A dynamical analysis of the rotation mechanism for conformational change in F1<\/sub>-ATPase, J. Ma, T. C. Flynn, Q. Cui, A. Leslie, J. E. Walker, M. Karplus, Structure, 10, 921-930 (2002)\u00a0<\/span>PDF version<\/a><\/p>\n

<\/a>33. Promoting modes and demoting modes in enzyme catalyzed proton transfer reactions: A study of models and realistic systems, Q. Cui, M. Karplus, J. Phys. Chem. B 106, 7927-7947 (2002)\u00a0<\/span>PDF version<\/a><\/p>\n

<\/a>32. QM\/MM Studies of the Triosephosphate Isomerase (TIM) Catalyzed Reactions: The effect of geometry and tunneling on proton transfer rate constants, Q. Cui, M. Karplus J. Am. Chem. Soc. 124, 3093 (2002)\u00a0<\/span>PDF version<\/a><\/p>\n

<\/a>31. QM\/MM Studies of the Triosephosphate Isomerase (TIM) Catalyzed Reactions: Verification of Methodology and Analysis of the Reaction Mechanisms, Q. Cui, M. Karplus J. Phys. Chem. B 106, 1768 (2002)\u00a0<\/span>PDF version<\/a><\/p>\n

<\/a>30. A theoretical analysis of the proton and hydride transfer in liver alcohol dehydrogenase (LADH), Q. Cui, M. Elstner, M. Karplus, J. Phys. Chem. B 106, 2721 (2002)\u00a0<\/span>PDF version<\/a><\/p>\n

<\/a>29. Substrate conformational transitions in the active site of chorismate mutase: Their role in the catalytic mechanism, H. Guo, Q. Cui, W. N. Lipscomb and M. Karplus, Proc. Natl. Acad. Sci. USA 98, 9032 (2001)\u00a0<\/span>PDF version<\/a><\/p>\n

<\/a>28. Triosephosphate Isomerase: A Theoretical Comparison of Alternative Pathways, Q. Cui, M. Karplus, J. Am. Chem. Soc. 123, 2284 (2001)\u00a0<\/span>PDF version<\/a><\/p>\n

<\/a>27. A QM\/MM Implementation of the Self-Consistent Charge Density Functional Tight Binding (SCC-DFTB) Method, Q. Cui, M. Elstner, E. Kaxiras, T. Frauenheim, M. Karplus, J. Phys. Chem. B 105, 569,(2001)\u00a0<\/span>PDF version<\/a><\/p>\n

<\/a>26. Molecular Properties from combined QM\/MM methods. II. Chemical shifts in large molecules. Q. Cui, M. Karplus, J. Phys. Chem. B 104, 3721 (2000)\u00a0<\/span>PDF version<\/a><\/p>\n

<\/a>25. Molecular Properties from combined QM\/MM methods. I. Analytical second derivative and vibrational calculations. Q. Cui, M. Karplus, J. Chem. Phys. 112, 1133 (2000)\u00a0<\/span>PDF version<\/a><\/p>\n","protected":false},"excerpt":{"rendered":"

39. Is “proton wire” concerted or step-wise? A model study of proton transfers in carbonic anhydrase, Q. Cui, M. Karplus, J. Phys. Chem. B 107, 1071-1078 (2003)\u00a0PDF version 38. Understanding the role of active-site residues in chorimsmate mutase catalysis from molecular dynamics simulations, H. Guo, Q. Cui, W. N. Lipscomb, M. Karplus, Angew. Chim. Intl. […]<\/p>\n","protected":false},"author":10766,"featured_media":0,"parent":153,"menu_order":4,"comment_status":"closed","ping_status":"closed","template":"","meta":[],"_links":{"self":[{"href":"https:\/\/sites.bu.edu\/cui-group\/wp-json\/wp\/v2\/pages\/164"}],"collection":[{"href":"https:\/\/sites.bu.edu\/cui-group\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/sites.bu.edu\/cui-group\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/sites.bu.edu\/cui-group\/wp-json\/wp\/v2\/users\/10766"}],"replies":[{"embeddable":true,"href":"https:\/\/sites.bu.edu\/cui-group\/wp-json\/wp\/v2\/comments?post=164"}],"version-history":[{"count":2,"href":"https:\/\/sites.bu.edu\/cui-group\/wp-json\/wp\/v2\/pages\/164\/revisions"}],"predecessor-version":[{"id":166,"href":"https:\/\/sites.bu.edu\/cui-group\/wp-json\/wp\/v2\/pages\/164\/revisions\/166"}],"up":[{"embeddable":true,"href":"https:\/\/sites.bu.edu\/cui-group\/wp-json\/wp\/v2\/pages\/153"}],"wp:attachment":[{"href":"https:\/\/sites.bu.edu\/cui-group\/wp-json\/wp\/v2\/media?parent=164"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}