Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Ronald Brudler"'
Autor:
Sheng Li, Ronald Brudler, Chris R. Gessner, Virgil L. Woods, Sammy Tyndall, Elizabeth D. Getzoff
Publikováno v:
Journal of Molecular Biology. 363:148-160
Photoactive yellow protein (PYP) is a small bacterial photoreceptor that undergoes a light-activated reaction cycle. PYP is also the prototypical Per-Arnt-Sim (PAS) domain. PAS domains, found in diverse multi-domain proteins from bacteria to humans,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c5e1502c6d980a04a013b3df33b8a03
https://doi.org/10.1016/j.jmb.2006.07.078
https://doi.org/10.1016/j.jmb.2006.07.078
Autor:
John A. Tainer, Minoru Kanehisa, Takeshi Todo, Ken-ichi Kucho, Victoria A. Roberts, Kenichi Hitomi, Hiroyuki Toh, Masahiro Ishiura, Hiromi Daiyasu, Elizabeth D. Getzoff, Ronald Brudler
Publikováno v:
Molecular Cell. 11(1):59-67
Cryptochrome flavoproteins, which share sequence homology with light-dependent DNA repair photolyases, function as photoreceptors in plants and circadian clock components in animals. Here, we coupled sequencing of an Arabidopsis cryptochrome gene wit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::47befe08ba7f70c7287da536a8cd5773
Publikováno v:
Nature Structural Biology. 8:265-270
To understand how proteins translate the energy of sunlight into defined conformational changes, we have measured the photocycle reactions of photoactive yellow protein (PYP) using time-resolved step scan Fourier transform infrared (FTIR) spectroscop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c45bedeebaebdb40fb0507e4161602c4
https://doi.org/10.1038/85021
https://doi.org/10.1038/85021
Autor:
Klaus Gerwert, Ronald Brudler
Publikováno v:
Photosynthesis Research. 55:261-266
It is shown that step-scan Fourier transform infrared spectroscopy can be applied to resolve the QA−QB → QAQB− transition in Rhodobacter sphaeroides reaction centres with a 5 µs time resolution. In the mid-infrared region (1900 – 1200 cm−1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e80eb5d2d1228e933a10066f757bdbce
https://doi.org/10.1023/a:1006034322353
https://doi.org/10.1023/a:1006034322353
Autor:
Ronald, Brudler, Kenichi, Hitomi, Hiromi, Daiyasu, Hiroyuki, Toh, Ken-ichi, Kucho, Masahiro, Ishiura, Minoru, Kanehisa, Victoria A, Roberts, Takeshi, Todo, John A, Tainer, Elizabeth D, Getzoff
Publikováno v:
Molecular cell. 11(1)
Cryptochrome flavoproteins, which share sequence homology with light-dependent DNA repair photolyases, function as photoreceptors in plants and circadian clock components in animals. Here, we coupled sequencing of an Arabidopsis cryptochrome gene wit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5dc6baea2543559dca92bb6677d9c2d3
https://pubmed.ncbi.nlm.nih.gov/12535521
https://pubmed.ncbi.nlm.nih.gov/12535521
Autor:
Terrence E. Meyer, David P. Millar, Tammy T. Woo, Ronald Brudler, G. Tollin, Elizabeth D. Getzoff, Ulrich K. Genick, Savitha Devanathan, Klaus Gerwert, Michael A. Cusanovich
Publikováno v:
Biochemistry. 39(44)
To understand in atomic detail how a chromophore and a protein interact to sense light and send a biological signal, we are characterizing photoactive yellow protein (PYP), a water-soluble, 14 kDa blue-light receptor which undergoes a photocycle upon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aae6506a866c22be4451acbb90dcb19c
https://pubmed.ncbi.nlm.nih.gov/11063584
https://pubmed.ncbi.nlm.nih.gov/11063584
Publikováno v:
Biochimica et biophysica acta. 1174(1)
The gene encoding the superoxide dismutase (SOD) of the thermophilic archaeon Sulfolobus acidocaldarius has been isolated and sequenced. Both the start site and the termination sites of the corresponding transcript were mapped. The deduced amino acid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::19ec4d133778601155db78da668608e0
https://pubmed.ncbi.nlm.nih.gov/8334170
https://pubmed.ncbi.nlm.nih.gov/8334170
Publikováno v:
Current Biology-CB
Current Biology-CB, Elsevier, 1999, 9 (11), pp.R416-R418. ⟨10.1016/S0960-9822(99)80257-7⟩
Current Biology-CB, Elsevier, 1999, 9 (11), pp.R416-R418. ⟨10.1016/S0960-9822(99)80257-7⟩
International audience; Recently determined structures of the oxygen-sensing heme domain of the bacterial protein FixL have revealed a new binding environment and signal transduction mechanism for heme; they have also provided new insights into the d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61008b086b02e7d815411329b8cf9915