Zobrazeno 1 - 10
of 50
pro vyhledávání: '"Daniel A. Keedy"'
Autor:
Liliana Guerrero, Ali Ebrahim, Blake T. Riley, Minyoung Kim, Qingqiu Huang, Aaron D. Finke, Daniel A. Keedy
Publikováno v:
Communications Biology, Vol 7, Iss 1, Pp 1-13 (2024)
Abstract Protein function hinges on small shifts of three-dimensional structure. Elevating temperature or pressure may provide experimentally accessible insights into such shifts, but the effects of these distinct perturbations on protein structures
Externí odkaz:
https://doaj.org/article/e42c6fd4a69446e6bede24cd36072ab8
Autor:
Ali Ebrahim, Blake T. Riley, Desigan Kumaran, Babak Andi, Martin R. Fuchs, Sean McSweeney, Daniel A. Keedy
Publikováno v:
IUCrJ, Vol 9, Iss 5, Pp 682-694 (2022)
The COVID-19 pandemic, instigated by the SARS-CoV-2 coronavirus, continues to plague the globe. The SARS-CoV-2 main protease, or Mpro, is a promising target for the development of novel antiviral therapeutics. Previous X-ray crystal structures of Mpr
Externí odkaz:
https://doaj.org/article/855a82556f8649e4b9e4a5bbd42477a0
Autor:
Liliana Guerrero, Ali Ebrahim, Blake T. Riley, Minyoung Kim, Qingqiu Huang, Aaron D. Finke, Daniel A. Keedy
Publikováno v:
bioRxiv
Protein function hinges on small shifts of three-dimensional structure. Elevating temperature or pressure may provide experimentally accessible insights into such shifts, but the effects of these distinct perturbations on protein structures have not
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2951eecc27d60dcf5a01464f6953badd
https://doi.org/10.1101/2023.05.02.538097
https://doi.org/10.1101/2023.05.02.538097
Autor:
Tamar Skaist Mehlman, Justin T Biel, Syeda Maryam Azeem, Elliot R Nelson, Sakib Hossain, Louise Dunnett, Neil G Paterson, Alice Douangamath, Romain Talon, Danny Axford, Helen Orins, Frank von Delft, Daniel A Keedy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::346524b683c022b2d51c6966a826cfec
https://doi.org/10.7554/elife.84632.sa2
https://doi.org/10.7554/elife.84632.sa2
Publikováno v:
PLoS Computational Biology, Vol 11, Iss 10, p e1004507 (2015)
Proteins must move between different conformations of their native ensemble to perform their functions. Crystal structures obtained from high-resolution X-ray diffraction data reflect this heterogeneity as a spatial and temporal conformational averag
Externí odkaz:
https://doaj.org/article/8a5c2f5cf60c4c25becdd9a2bd92bf5c
Autor:
Daniel A. Keedy
Publikováno v:
Acta Crystallographica. Section D, Structural Biology
Crystallography at multiple temperatures can reveal the collective shifts of alternative conformations that underlie allosteric communication through protein structures.
Proteins inherently fluctuate between conformations to perform functions in
Proteins inherently fluctuate between conformations to perform functions in
Publikováno v:
bioRxiv
The COVID-19 pandemic, instigated by the SARS-CoV-2 coronavirus, continues to plague the globe. The SARS-CoV-2 main protease, or Mpro, is a promising target for development of novel antiviral therapeutics. Previous X-ray crystal structures of Mpro we
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::18396e458afdc4db2e21f3640ae81679
https://doi.org/10.1101/2021.05.03.437411
https://doi.org/10.1101/2021.05.03.437411
Autor:
Henry van den Bedem, Stephanie A. Wankowicz, Daniel A. Keedy, Blake T. Riley, Daniel W. Hogan, Saulo H. P. de Oliveira, James S. Fraser, Gydo C. P. van Zundert
Publikováno v:
Protein Sci
New X-ray crystallography and cryo-electron microscopy (cryo-EM) approaches yield vast amounts of structural data from dynamic proteins and their complexes. Modeling the full conformational ensemble can provide important biological insights, but iden
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::921656bc23ed6d23df348820b166c701
https://europepmc.org/articles/PMC7737783/
https://europepmc.org/articles/PMC7737783/
Autor:
Daniel A Keedy, Ivelin Georgiev, Edward B Triplett, Bruce R Donald, David C Richardson, Jane S Richardson
Publikováno v:
PLoS Computational Biology, Vol 8, Iss 8, p e1002629 (2012)
Amino acid substitutions in protein structures often require subtle backbone adjustments that are difficult to model in atomic detail. An improved ability to predict realistic backbone changes in response to engineered mutations would be of great uti
Externí odkaz:
https://doaj.org/article/0fafa1920b8342ebad92d96d402abcb8
Autor:
W. Bryan Arendall, Paul D. Adams, Lizbeth L. Videau, Swati Jain, Jack Snoeyink, Steven M. Lewis, Bradley J. Hintze, Daniel A. Keedy, Vishal Verma, Lindsay N. Deis, Jeffrey J. Headd, Michael G. Prisant, David S. Richardson, Nigel W. Moriarty, Simon C. Lovell, Jane S. Richardson, Vincent B. Chen, Christopher J. Williams
Publikováno v:
Protein Science. 27:293-315
This paper describes the current update on macromolecular model validation services that are provided at the MolProbity website, emphasizing changes and additions since the previous review in 2010. There have been many infrastructure improvements, in