Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Frank P. Sharples"'
Autor:
Tomáš Polívka, Harry A. Frank, Timothy W. Chapp, Robielyn P. Ilagan, Frank P. Sharples, Roger G. Hiller
Publikováno v:
Photosynthesis Research
Low temperature, steady-state, optical spectroscopic methods were used to study the spectral features of peridinin-chlorophyll-protein (PCP) complexes in which recombinant apoprotein has been refolded in the presence of peridinin and either chlorophy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2cb94787cf13159373a98cacc2f0dfbc
http://europepmc.org/articles/PMC1769343
http://europepmc.org/articles/PMC1769343
Autor:
Roger G. Hiller, Julian Catmull, Frank P. Sharples, Robert Puskeiler, David J. Miller, Helen Tweedale
Publikováno v:
Photosynthesis Research. 86:229-240
The coding regions for the N-domain, and full length peridinin-chlorophyll a apoprotein (full length PCP), were expressed in Escherichia coli. The apoproteins formed inclusion bodies from which the peptides could be released by hot buffer. Both the a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::449fcb879fd095f7f9ed465d17916607
https://doi.org/10.1007/pl00022067
https://doi.org/10.1007/pl00022067
Autor:
Tomáš Polívka, Harry A. Frank, Villy Sundström, Frank P. Sharples, Roger G. Hiller, Donatas Zigmantas
Publikováno v:
Phys. Chem. Chem. Phys.. 6:3009-3016
Effects of introducing a carbonyl group into the conjugation system of carotenoids were studied for four naturally occurring carotenoids: peridinin, fucoxanthin, siphonaxanthin and spheroidenone. The conjugated carbonyl group affects energetics and d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::11b00d10404f8d855ddec894c0198e6e
https://doi.org/10.1039/b315786e
https://doi.org/10.1039/b315786e
Autor:
Frank P. Sharples, Sumie Shima, Robielyn P. Ilagan, Nathan B. Gillespie, Harry A. Frank, Roger G. Hiller, Brandi J. Sommer, Robert R. Birge
Publikováno v:
The Journal of Physical Chemistry A. 107:8052-8066
The ground and excited-state properties of peridinin in solution and in the peridinin-chlorophyll-protein (PCP) complex are studied by using one-photon and two-photon spectroscopy, solvent effects, and quantum theory. Two-photon excitation spectra, t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::48296b25d55400fbd5116d94908fc8a8
https://doi.org/10.1021/jp022648z
https://doi.org/10.1021/jp022648z
Autor:
Michael R. Wasielewski, Roger G. Hiller, David J. Gosztola, James A. Bautista, Jesusa S. Josue, Harry A. Frank, Frank P. Sharples, Zeus Pendon
Publikováno v:
The Journal of Physical Chemistry B. 104:4569-4577
The spectroscopic properties and dynamics of the lowest excited singlet states of peridinin, fucoxanthin, neoxanthin, uriolide acetate, spheroidene, and spheroidenone in several different solvents have been studied by steady-state absorption and fast
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5f7e3d5c337b69d3db961169aad9318d
https://doi.org/10.1021/jp000079u
https://doi.org/10.1021/jp000079u
Autor:
Robert E. Connors, David J. Gosztola, B. Bangar Raju, Frank P. Sharples, James A. Bautista, Roger G. Hiller, Harry A. Frank, Michael R. Wasielewski
Publikováno v:
The Journal of Physical Chemistry B. 103:8751-8758
The spectroscopic properties and dynamic behavior of peridinin in several different solvents were studied by steady-state absorption, fluorescence, and transient optical spectroscopy. The lifetime of the lowest excited singlet state of peridinin is f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ade7b5a37ef7b41c0733a14c933d5d29
https://doi.org/10.1021/jp9916135
https://doi.org/10.1021/jp9916135
Singlet and Triplet Energy Transfer in the Peridinin−Chlorophyll a−Protein from Amphidinium carterae
Autor:
Roger G. Hiller, David J. Gosztola, Michael R. Wasielewski, Frank P. Sharples, Harry A. Frank, James A. Bautista
Publikováno v:
The Journal of Physical Chemistry A. 103:2267-2273
The spectroscopic properties of peridinin in solution, and the efficiency and dynamics of energy transfer from peridinin to chlorophyll a in the peridinin-chlorophyll-protein (PCP) from Amphidinium carterae, were studied by steady-state absorption, f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::27acc0e68513bd9786c53cf56208402a
https://doi.org/10.1021/jp983943f
https://doi.org/10.1021/jp983943f
Publikováno v:
FEBS Letters. 363:175-178
The principle light-harvesting chlorophyll a-c-binding protein of Amphidinium carterae of 19 kDa is encoded as a polyprotein translated from a 6.1 kb mRNA. The cDNA sequences indicate that each derived polypeptide is contiguous with the next and that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b18c1b2d7bb4e4bdb20db3b4328d823
https://doi.org/10.1016/0014-5793(95)00297-m
https://doi.org/10.1016/0014-5793(95)00297-m
Publikováno v:
Biochemistry. 48(21)
Light-harvesting complexes have evolved into very different structures but fulfill the same function, efficient harvesting of solar energy. In these complexes, pigments are fine-tuned and properly arranged to gather incoming photons. In the photosynt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::633042ff7622da85cbbe1c499dc40a18
https://pubmed.ncbi.nlm.nih.gov/19371099
https://pubmed.ncbi.nlm.nih.gov/19371099
Autor:
Robert R. Birge, Robielyn P. Ilagan, Harry A. Frank, Frank P. Sharples, George N. Gibson, Roger G. Hiller, Jeremy F. Koscielecki
Publikováno v:
Biochemistry. 45(47)
Steady-state and femtosecond time-resolved optical methods have been used to compare the spectroscopic features and energy transfer dynamics of two systematically different light-harvesting complexes from the dinoflagellate Amphidinium carterae: main
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::743c1c83a726e076a22223460e2151ca
https://pubmed.ncbi.nlm.nih.gov/17115700
https://pubmed.ncbi.nlm.nih.gov/17115700