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    Wyświetlanie 1-3 z 3
    Tytuł:
    Spectroscopy of Photosynthetic Pigment-Protein Complex LHCII
    Autorzy:
    Gruszecki, W.
    Zubik, M.
    Luchowski, R.
    Grudzinski, W.
    Gryczynski, Z.
    Gryczynski, I.
    Powiązania:
    https://bibliotekanauki.pl/articles/1490052.pdf
    Data publikacji:
    2012-02
    Wydawca:
    Polska Akademia Nauk. Instytut Fizyki PAN
    Tematy:
    87.64.-t
    Opis:
    Light-harvesting pigment-protein complex of photosystem II is the most abundant membrane protein in the biosphere, comprising more than half chlorophyll molecules. The protein plays a role of photosynthetic antenna, collecting solar radiation and transferring excitations towards the reaction centers, where electric charge separation takes place. Efficient excitation energy capture and transfer requires unique organization of the complex and unique photophysical properties of the accessory pigments: chlorophylls and carotenoids. LHCII is also a place where extremely harmful singlet oxygen may be generated, under strong illumination conditions. Several physical mechanisms have been found in LHCII, operating to protect the photosynthetic apparatus against light-induced damage, including chlorophyll triplet and singlet excitations quenching by carotenoids. In this paper we discuss the results of our recent studies, carried out with the application of several molecular spectroscopy techniques (electronic absorption, fluorescence, resonance Raman and FTIR), designed to investigate molecular mechanisms responsible for regulation of excitation density in LHCII. Among the most interesting findings are the light-induced molecular configuration changes of the LHCII-bound xanthophylls, leading to conformational rearrangements of the protein. These mechanisms are discussed in terms of excessive excitation quenching in the pigment-protein complex subjected to overexcitation. Such an activity seems to represent a vital regulatory process in the photosynthetic apparatus, at the molecular level, protecting plants against photodegradation.
    Źródło:
    Acta Physica Polonica A; 2012, 121, 2; 397-400
    0587-4246
    1898-794X
    Pojawia się w:
    Acta Physica Polonica A
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Numerical experiments with model equations of cancer invasion of tissue
    Autorzy:
    Kolev, M.
    Zubik-Kowal, B.
    Powiązania:
    https://bibliotekanauki.pl/articles/206179.pdf
    Data publikacji:
    2011
    Wydawca:
    Polska Akademia Nauk. Instytut Badań Systemowych PAN
    Tematy:
    in vivo tumorigenicity
    cancer cells
    proliferation
    chemotaxis
    haptotaxis
    extracellular matrix
    tumour invasion
    mathematical model
    animal models
    approximations
    Opis:
    In this paper we investigate a mathematical model of cancer invasion of tissue, which incorporates haptotaxis, chemotaxis, proliferation and degradation rates for cancer cells and the extracellular matrix, kinetics of urokinase receptor, and urokinase plasminogen activator cycle. We solve the model using spectrally accurate approximations and compare its numerical solutions with laboratory data. The spectral accuracy allows to use low-dimensional matrices and vectors, which speeds up the computations of the numerical solutions and thus to estimate the parameter values for the model equations. Our numerical results demonstrate correlations between numerical data computed from the mathematical model and in vivo tumour growth rates from prostate cell lines.
    Źródło:
    Control and Cybernetics; 2011, 40, 3; 779-791
    0324-8569
    Pojawia się w:
    Control and Cybernetics
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Comparative Analysis of KP-HSA Complex by Spectroscopic Methods
    Autorzy:
    Mąciażek-Jurczyk, M.
    Równicka-Zubik, J.
    Dyja, R.
    Sułkowska, A.
    Powiązania:
    https://bibliotekanauki.pl/articles/1400125.pdf
    Data publikacji:
    2013-04
    Wydawca:
    Polska Akademia Nauk. Instytut Fizyki PAN
    Tematy:
    33.50.-j
    33.50.Dq
    82.56.-b
    87.14.-g
    87.14.E-
    Opis:
    The main objective of the presented study was to characterize the high (HAS) and low affinity (LAS) binding sites of ketoprofen (KP) in human serum albumin (HSA) structure with the use of spectrofluorescence and proton nuclear magnetic resonance spectroscopy. In vitro fluorescence analysis was used to estimate the effect of KP on the HSA fluorescence. The association constants $K_{a} [M^{-1}]$ of KP-HSA complex in the HAS were determined with the use of Scatchard, Klotz, and Hill analysis. The quenching $K_{Q} [M^{-1}]$ constants were determined on the basis of the Stern-Volmer equation. Binding of ketoprofen to plasma protein was also studied with the use of 8-anilinonapthalene-1-sulfonic acid (ANS) and 5-dimethylaminonaphthalene-1-sulfonic acid (DNSA) as the fluorescence probes in IIIA and IIA subdomains of HSA, respectively. To estimate the cooperativeness in proteins Hill's coefficient $n_{H}$ was used. The analysis of proton nuclear magnetic resonance spectra of KP in the presence of HSA allows us to observe the interactions between aromatic rings of the drug and the rings of amino acids located in the hydrophobic subdomains of the protein on the basis of the changes of chemical shifts Δ σ [ppm] of drug protons resonances. Moreover the $K_{a}$ constants $[M^{-1}]$ of KP-HSA complex in the LAS were determined.
    Źródło:
    Acta Physica Polonica A; 2013, 123, 4; 673-680
    0587-4246
    1898-794X
    Pojawia się w:
    Acta Physica Polonica A
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-3 z 3

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