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:
Stephanie A Wankowicz, Ashraya Ravikumar, Shivani Sharma, Blake Riley, Akshay Raju, Daniel W Hogan, Jessica Flowers, Henry van den Bedem, Daniel A Keedy, James S Fraser
Publikováno v:
eLife, Vol 12 (2024)
In their folded state, biomolecules exchange between multiple conformational states that are crucial for their function. Traditional structural biology methods, such as X-ray crystallography and cryogenic electron microscopy (cryo-EM), produce densit
Externí odkaz:
https://doaj.org/article/df7cabe4cceb4472bbdd8fd7453b61bf
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:
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
Publikováno v:
eLife, Vol 12 (2023)
Much of our current understanding of how small-molecule ligands interact with proteins stems from X-ray crystal structures determined at cryogenic (cryo) temperature. For proteins alone, room-temperature (RT) crystallography can reveal previously hid
Externí odkaz:
https://doaj.org/article/aac320db06f049d18577b3ebd803e700
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
Autor:
Daniel A Keedy, Zachary B Hill, Justin T Biel, Emily Kang, T Justin Rettenmaier, José Brandão-Neto, Nicholas M Pearce, Frank von Delft, James A Wells, James S Fraser
Publikováno v:
eLife, Vol 7 (2018)
Allostery is an inherent feature of proteins, but it remains challenging to reveal the mechanisms by which allosteric signals propagate. A clearer understanding of this intrinsic circuitry would afford new opportunities to modulate protein function.
Externí odkaz:
https://doaj.org/article/f31e59e6c613444c8e3b921c3cf0906f
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, Lillian R Kenner, Matthew Warkentin, Rahel A Woldeyes, Jesse B Hopkins, Michael C Thompson, Aaron S Brewster, Andrew H Van Benschoten, Elizabeth L Baxter, Monarin Uervirojnangkoorn, Scott E McPhillips, Jinhu Song, Roberto Alonso-Mori, James M Holton, William I Weis, Axel T Brunger, S Michael Soltis, Henrik Lemke, Ana Gonzalez, Nicholas K Sauter, Aina E Cohen, Henry van den Bedem, Robert E Thorne, James S Fraser
Publikováno v:
eLife, Vol 4 (2015)
Determining the interconverting conformations of dynamic proteins in atomic detail is a major challenge for structural biology. Conformational heterogeneity in the active site of the dynamic enzyme cyclophilin A (CypA) has been previously linked to i
Externí odkaz:
https://doaj.org/article/20ede3c217614534b0cc830dee6b77a3
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4181b3d16ef5de87fecfd665706eb6c9
https://doi.org/10.1107/s2059798318017941
https://doi.org/10.1107/s2059798318017941