Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Crystal E. Valdez"'
Publikováno v:
The journal of physical chemistry. B, vol 119, iss 19
Nechay, MR; Valdez, CE; & Alexandrova, AN. (2015). Computational treatment of metalloproteins. Journal of Physical Chemistry B, 119(19), 5945-5956. doi: 10.1021/acs.jpcb.5b00028. UCLA: Retrieved from: http://www.escholarship.org/uc/item/0099h0w7
Nechay, MR; Valdez, CE; & Alexandrova, AN. (2015). Computational treatment of metalloproteins. Journal of Physical Chemistry B, 119(19), 5945-5956. doi: 10.1021/acs.jpcb.5b00028. UCLA: Retrieved from: http://www.escholarship.org/uc/item/0099h0w7
© 2015 American Chemical Society. Metalloproteins present a considerable challenge for modeling, especially when the starting point is far from thermodynamic equilibrium. Examples include formidable problems such as metalloprotein folding and struct
Autor:
Donna J. Nelson, H. N. Cheng, Alison K. Hall, Gail P. Taylor, J. Aaron Cassill, Edwin J. Barea-Rodriguez, Stassi DiMaggio, Melissa S. Kosinski-Collins, Kim Godsoe, Irving R. Epstein, Jean Chmielewski, Colby M. Adolph, Stella K. Betancourt, Reena Blade, Christopher J. Pulliam, Dontarie Stallings, Srikant Iyer, Rigoberto Hernandez, David R. Brown, William A. Lester, Paris Svoronos, Luis A. Colón, Todd Pagano, Gloria A. Thomas, Zakiya S. Wilson-Kennedy, Crystal E. Valdez, Steven A. Lopez, Pratibha Varma-Nelson, Sibrina N. Collins, Christopher J. Bannochie, Allen A. Denio, Karl S. Booksh, Ashley Neybert, Ellene Tratras Contis, Ricardo McKlmon, Bradley D. Miller
Autor:
Steven A. Lopez, Crystal E. Valdez
Publikováno v:
ACS Symposium Series ISBN: 9780841232365
ACS Symposium Series
ACS Symposium Series
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5afc7a51aab9173cdb86b9a27155394f
https://doi.org/10.1021/bk-2017-1256.ch013
https://doi.org/10.1021/bk-2017-1256.ch013
Publikováno v:
Chemical Physics Letters. 604:77-82
Acireductone dioxygenase (ARD) oxidizes 1,2-dihydroxy-3-keto-5-(methylthio)pentene to either formate and an α-keto acid, or formate, methylthiopropionate and CO, depending on the nature of the catalytic metal, Fe 2+ or Ni 2+ . We recently showed tha
Publikováno v:
Physical chemistry chemical physics : PCCP, vol 18, iss 46
Valdez, CE; Morgenstern, A; Eberhart, ME; & Alexandrova, AN. (2016). Predictive methods for computational metalloenzyme redesign-a test case with carboxypeptidase A. PHYSICAL CHEMISTRY CHEMICAL PHYSICS, 18(46), 31744-31756. doi: 10.1039/c6cp02247b. UCLA: Retrieved from: http://www.escholarship.org/uc/item/4wh1q407
Valdez, CE; Morgenstern, A; Eberhart, ME; & Alexandrova, AN. (2016). Predictive methods for computational metalloenzyme redesign-a test case with carboxypeptidase A. PHYSICAL CHEMISTRY CHEMICAL PHYSICS, 18(46), 31744-31756. doi: 10.1039/c6cp02247b. UCLA: Retrieved from: http://www.escholarship.org/uc/item/4wh1q407
Computational metalloenzyme design is a multi-scale problem. It requires treating the metal coordination quantum mechanically, extensive sampling of the protein backbone, and additionally accounting for the polarization of the active site by both the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::edc7975d849239097a95670e55e62df9
https://escholarship.org/uc/item/4wh1q407
https://escholarship.org/uc/item/4wh1q407
Publikováno v:
Accounts of chemical research, vol 47, iss 10
Valdez, CE; Smith, QA; Nechay, MR; & Alexandrova, AN. (2014). Mysteries of metals in metalloenzymes. Accounts of Chemical Research, 47(10), 3110-3117. doi: 10.1021/ar500227u. UCLA: Retrieved from: http://www.escholarship.org/uc/item/0nw1f253
Valdez, CE; Smith, QA; Nechay, MR; & Alexandrova, AN. (2014). Mysteries of metals in metalloenzymes. Accounts of Chemical Research, 47(10), 3110-3117. doi: 10.1021/ar500227u. UCLA: Retrieved from: http://www.escholarship.org/uc/item/0nw1f253
© 2014 American Chemical Society. ConspectusNatural metalloenzymes are often the most proficient catalysts in terms of their activity, selectivity, and ability to operate at mild conditions. However, metalloenzymes are occasionally surprising in the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2890a53223e8023db323a7862d71acb1
https://escholarship.org/uc/item/0nw1f253
https://escholarship.org/uc/item/0nw1f253
Publikováno v:
Journal of molecular biology, vol 425, iss 16
Sparta, M; Valdez, CE; & Alexandrova, AN. (2013). Metal-dependent activity of Fe and Ni acireductone dioxygenases: How two electrons reroute the catalytic pathway. Journal of Molecular Biology, 425(16), 3007-3018. doi: 10.1016/j.jmb.2013.05.001. UCLA: Retrieved from: http://www.escholarship.org/uc/item/8d45m192
Sparta, M; Valdez, CE; & Alexandrova, AN. (2013). Metal-dependent activity of Fe and Ni acireductone dioxygenases: How two electrons reroute the catalytic pathway. Journal of Molecular Biology, 425(16), 3007-3018. doi: 10.1016/j.jmb.2013.05.001. UCLA: Retrieved from: http://www.escholarship.org/uc/item/8d45m192
Two virtually identical acireductone dioxygenases, ARD and ARD′, catalyze completely different oxidation reactions of the same substrate, 1,2-dihydroxy-3-keto-5-(methylthio)pentene, depending exclusively on the nature of the bound metal. Fe2 +-depe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3131f6dcac93ccbd7cf04f4d1dd0d38c
https://escholarship.org/uc/item/8d45m192
https://escholarship.org/uc/item/8d45m192
Publikováno v:
The journal of physical chemistry. B. 116(35)
Ureases and metallo-β-lactamases are amide hydrolases closely related in function and structure. However, one major difference between them is that the former uses two nickel cations, and the latter uses two zinc cations to do similar catalytic jobs
Publikováno v:
Journal of Physical Chemistry B; May2015, Vol. 119 Issue 19, p5945-5956, 12p