Zobrazeno 1 - 10
of 88
pro vyhledávání: '"Brian R. Gibney"'
Autor:
Naty Barak, Brian R. Gibney, Paul Westerhof, Diana Bauer, F. Todd Davidson, Spiro D. Alexandratos, Susan S. Hubbard, Hessy L. Taft
Publikováno v:
ACS Sustainable Chemistry & Engineering. 7:2879-2888
Water is essential to human health and economic development due to its utilization in sanitation, agriculture, and energy. Supplying water to an expanding world population requires simultaneous consideration of multiple societal sectors competing for
Autor:
Brian R. Gibney
Publikováno v:
Encyclopedia of Biophysics ISBN: 9783642359439
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3629032113a347e06f3ffddefdbaf1f5
https://doi.org/10.1007/978-3-642-35943-9_43-1
https://doi.org/10.1007/978-3-642-35943-9_43-1
Publikováno v:
Inorganic Chemistry. 54:5942-5948
Zinc finger transcription factors are the largest class of metalloproteins in the human genome. Binding of Zn(II) to their canonical Cys2His2, Cys3His1, or Cys4 sites results in metal-induced protein folding events required to achieve their biologica
Autor:
Inna Bakman, Amy R. Marts, Terry L. Dowd, Brian R. Gibney, Ka Lam Chan, David L. Tierney, Yuksel Batir
Publikováno v:
Inorganic Chemistry
Zinc finger proteins that bind Zn(II) using a Cys2His2 coordination motif within a ββα protein fold are the most abundant DNA binding transcription factor domains in eukaryotic systems. These classic zinc fingers are typically unfolded in the apo
Autor:
Brian R. Gibney
Complete thermodynamic descriptions of the interactions of cofactors with proteins via equilibrium studies are challenging, but are essential to the evaluation of designed metalloproteins. While decades of studies on protein-protein interaction therm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::57357526d51b086e66483d9004e557cc
https://doi.org/10.1016/bs.mie.2016.06.002
https://doi.org/10.1016/bs.mie.2016.06.002
Autor:
Cheryl A. Kerfeld, Brian R. Gibney, Eric L. Hegg, Clement Aussignargues, Markus Sutter, Jefferson S. Plegaria, Aiko Turmo, Maria-Eirini Pandelia, Jan Zarzycki, Daniel C. Ducat, Jingcheng Huang
Publikováno v:
Journal of the American Chemical Society. 138(16)
Bacterial microcompartments (BMCs) are self-assembling organelles composed of a selectively permeable protein shell and encapsulated enzymes. They are considered promising templates for the engineering of designed bionanoreactors for biotechnology. I
Autor:
Pierre Moënne-Loccoz, Brian R. Gibney, Xiaoli Shi, Alisha M. Thompson, Robert A. Goldbeck, Amit R. Reddi, Theodore R. Holman
Publikováno v:
Biochemistry. 46:14629-14637
Current studies on the Saccharomyces cerevisiae protein Dap1p have demonstrated a heme-related function within the ergosterol biosynthetic pathway. Here we present data to further the understanding of the role of heme in the proper biological functio
Publikováno v:
Nucleic Acids Research
Proteins containing heme, iron(protoporphyrin IX) and its variants, continue to be one of the most-studied classes of biomolecules due to their diverse range of biological functions. The literature is abundant with reports of structural and functiona
Publikováno v:
Journal of the American Chemical Society. 129:12815-12827
Zinc finger transcription factors represent the largest single class of metalloproteins in the human genome. Binding of Zn(II) to their canonical Cys4, Cys3His1, or Cys2His2 sites results in metal-induced protein folding events required to achieve th
Publikováno v:
Biochemistry. 46:291-305
To study the engineering requirements for proton pumping in energy-converting enzymes such as cytochrome c oxidase, the thermodynamics and mechanisms of proton-coupled electron transfer in two designed heme proteins are elucidated. Both heme protein