Informacja

Drogi użytkowniku, aplikacja do prawidłowego działania wymaga obsługi JavaScript. Proszę włącz obsługę JavaScript w Twojej przeglądarce.

English (EN)·Polski (PL)·Yкраїнський (UK)
Przejdź do strony domowej biblioteki Centralna Biblioteka Wojskowa Link otwiera się w nowym oknie Logo biblioteki Prolib Integro - strona głównaCentralna Biblioteka Wojskowa

Wyszukujesz frazę "atomic microscopy" wg kryterium: Temat

  Lista filtrów
Wyrównaj
    Wyświetlanie 1-4 z 4
    Tytuł:
    The effect of Galleria mellonella hemolymph polypeptides on Legionella gormanii
    Autorzy:
    Chmiel, Elżbieta
    Palusinska-Szysz, Marta
    Zdybicka-Barabas, Agnieszka
    Cytryńska, Małgorzata
    Mak, Paweł
    Powiązania:
    https://bibliotekanauki.pl/articles/1039350.pdf
    Data publikacji:
    2014
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    Legionella gormanii
    Galleria mellonella
    apolipophorin III
    Atomic Force Microscopy
    Opis:
    Among Legionella species, which are recognized to be pathogenic for humans, L. gormanii is the second prevalent causative agent of community-acquired pneumonia after L. pneumophila. Anti-L. gormanii activity of Galleria mellonella hemolymph extract and apolipophorin III (apoLp-III) was examined. The extract and apoLp-III at the concentration 0.025 mg/ml caused 75% and 10% decrease of the bacteria survival rate, respectively. The apoLp-III-induced changes of the bacteria cell surface were analyzed for the first time by atomic force microscopy. Our studies demonstrated the powerful anti-Legionella effects of the insect defence polypeptides, which could be exploited in drugs design against these pathogens.
    Źródło:
    Acta Biochimica Polonica; 2014, 61, 1; 123-127
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Atomic force microscopy studies of the adhesive properties of DPPC vesicles containing β-carotene
    Autorzy:
    Augustyńska, Dominika
    Jemioła-Rzemińska, Małgorzata
    Burda, Kvetoslava
    Strzałka, Kazimierz
    Powiązania:
    https://bibliotekanauki.pl/articles/1039795.pdf
    Data publikacji:
    2012
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    atomic force microscopy
    dipalmitoylphosphatidylcholine
    β-carotene
    liposome adhesion
    thermal transition
    Opis:
    A role of carotenoids as modulators of physical properties of model and biological membranes has been already postulated. However, there is a lack of information on the influence of these pigments on interactions between the lipids which form such membranes. This paper applies atomic force microscopy (AFM) in to study the effects of β-carotene on the adhesion properties of DPPC multilamellar liposomes. This allowed us to gain, for the first time, a direct insight into the interactions between the components in model systems on a molecular level. We observe that the adhesive forces in DPPC multilamellar liposomes containing 1mol% of β-carotene decrease exponentially with increasing temperature, and that at about 37°C they diminish. In the case of pure liposomes the decline in adhesion is of a different nature and the adhesive forces disappear at 34°C. The adhesive forces are about 5 times higher at 31°C in the presence of β-carotene than in its absence. However, measurements using differential scanning calorimetry (DSC) showed a shift of the lamellar-to-undulled-lamellar phase transition toward lower temperatures by about 0.8±0.2°C in a system containing β-carotene. The enthalpy changes (ΔH) of this transition are similar for both systems. For the main transition, gel-to-liquid crystalline, the peak is shifted by about 0.5±0.1°C, and ΔH decreases by about 30% in liposomes treated with β-carotene in comparison to pure liposomes. Our results suggest increased cooperation between liposome components in a system with enriched β-carotene, which cause a change in phase transition temperatures. Moreover, these interactions are very sensitive to temperature.
    Źródło:
    Acta Biochimica Polonica; 2012, 59, 1; 125-128
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Dynamic force measurements of avidin-biotin and streptavdin-biotin interactions using AFM
    Autorzy:
    de Odrowąż Piramowicz, Marzena
    Czuba, Paweł
    Targosz, Marta
    Burda, Kvĕtoslava
    Szymoński, Marek
    Powiązania:
    https://bibliotekanauki.pl/articles/1041274.pdf
    Data publikacji:
    2006
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    atomic force microscopy
    rupture force
    loading rate
    streptavidin
    avidin
    biotin
    dissociation rate
    Opis:
    Using atomic force microscopy (AFM) we performed dynamic force measurements of the adhesive forces in two model systems: avidin-biotin and streptavidin-biotin. In our experiments we used glutaraldehyde for immobilization of (strept)avidin on the tip and biotin on the sample surface. Such interface layers are more rigid than those usually reported in the literature for AFM studies, when (strept)avidin is coupled with biotinylated bovine albumin and biotin with agarose polymers. We determined the dependence of the rupture forces of avidin-biotin and streptavidin-biotin bonds in the range 300-9600 pN/s. The slope of a semilogarithmic plot of this relation changes at about 1700 pN/s. The existence of two different regimes indicates the presence of two activation barriers of these complexes during the dissociation process. The dissociation rates and activation energy barriers, calculated from the Bell model, for the avidin-biotin and streptavidin-biotin interactions are similar to each other for loading rates >1700 pN/s but they are different from each other for loading rates < 1700 pN/s. In the latter case, the dissociation rates show a higher stability of the avidin-biotin complex than the streptavidin-biotin complex due to a larger outer activation barrier of 0.8 kBT. The bond-rupture force is about 20 pN higher for the avidin-biotin pair than for the streptavidin-biotin pair for loading rates < 1700 pN/s. These two experimental observations are in agreement with the known structural differences between the biotin binding pocket of avidin and of streptavidin.
    Źródło:
    Acta Biochimica Polonica; 2006, 53, 1; 93-100
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Insertion of GPI-anchored alkaline phosphatase into supported membranes: a combined AFM and fluorescence microscopy study.
    Autorzy:
    Rieu, Jean-Paul
    Ronzon, Frédéric
    Place, Christophe
    Dekkiche, Fairouz
    Cross, Benjamin
    Roux, Bernard
    Powiązania:
    https://bibliotekanauki.pl/articles/1043341.pdf
    Data publikacji:
    2004
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    fluorescent beads
    atomic force microscopy (AFM)
    GPI anchors
    alkaline phosphatase
    supported lipid membranes
    Opis:
    A new method based on combined atomic force microscopy (AFM) and fluorescence microscopy observations, is proposed to visualize the insertion of glycosylphosphatidyl inositol (GPI) anchored alkaline phosphatase from buffer solutions into supported phospholipid bilayers. The technique involves the use of 27 nm diameter fluorescent latex beads covalently coupled to the amine groups of proteins. Fluorescence microscopy allows the estimation of the relative protein coverage into the membrane and also introduces a height amplification for the detection of protein/bead complexes with the AFM. The coupling of the beads with the amine groups is not specific; this new and simple approach opens up new ways to investigate proteins into supported membrane systems.
    Źródło:
    Acta Biochimica Polonica; 2004, 51, 1; 189-197
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-4 z 4

      Ta witryna wykorzystuje pliki cookies do przechowywania informacji na Twoim komputerze. Pliki cookies stosujemy w celu świadczenia usług na najwyższym poziomie, w tym w sposób dostosowany do indywidualnych potrzeb. Korzystanie z witryny bez zmiany ustawień dotyczących cookies oznacza, że będą one zamieszczane w Twoim komputerze. W każdym momencie możesz dokonać zmiany ustawień dotyczących cookies