Temat: 82.39.Pj - Katalog OPAC zbiorów

Skocz do pozycji: 1.

Tytuł:: Study of Probes and Substrates for Low Temperature Atomic Force Microscopy and Biological Applications
Autorzy:: Radenovic, A.
Bystrenova, E.
Libioulle, L.
Dietler, G.
Powiązania:: https://bibliotekanauki.pl/articles/2036949.pdf
Data publikacji:: 2003
Wydawca:: Polska Akademia Nauk. Instytut Fizyki PAN
Tematy:: 07.79.Lh
68.37.Hk
82.39.Pj
07.20.Mc
Opis:: The atomic force microscopy in ultrahigh vacuum and at low temperature demonstrated its excellent capability to reach atomic resolution. Nevertheless in the case of biological samples high resolution has been achieved only in very few cases. We demonstrated here the importance of the appropriate choice of probes and substrates in order to image DNA at low temperature with high resolution. We investigated properties of three types of cantilevers and they were studied by scanning electron microscopy as a function of temperature. A large bending of cantilevers, which were coated from both sides, was observed at low temperatures. Therefore uncoated cantilevers are strongly recommended for low temperature applications. Different methods for immobilization of DNA on the substrate are examined at low temperatures. First images of linear DNA on graphite at 82 K under ultrahigh vacuum conditions are presented.
Źródło:: Acta Physica Polonica A; 2003, 104, 3-4; 373-380
0587-4246
1898-794X
Pojawia się w:: Acta Physica Polonica A
Dostawca treści:: Biblioteka Nauki

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Skocz do pozycji: 2.

Tytuł:: Mössbauer Studies of Cu(II) Ions Interaction with the Non-Heme Iron and Cytochrome b$\text{}_{559}$ in a Chlamydomonas reinhardtii PSI Minus Mutant
Autorzy:: Burda, K.
Kruk, J.
Strzałka, K.
Stanek, J.
Schmid, G. H.
Kruse, O.
Powiązania:: https://bibliotekanauki.pl/articles/2044646.pdf
Data publikacji:: 2006-03
Wydawca:: Polska Akademia Nauk. Instytut Fizyki PAN
Tematy:: 82.39.Jn
82.39.Rt
82.50.Nd
87.15.He
87.64.Pj
89.60.Fe
Opis:: Mössbauer spectroscopy was applied, for the first time, to study the interaction of copper ions with the non-heme iron and the heme iron of cytochrome b$\text{}_{559}$ in photosystem II thylakoids isolated from a Chlamydomonas reinhardtii photosystem I minus mutant. We showed that copper ions oxidize the heme iron and change its low spin state into a high spin state. This is probably due to deprotonation of the histidine coordinating the heme. We also found that copper preserves the non-heme iron in a low spin ferrous state, enhancing the covalence of iron bonds as compared to the untreated sample. We suggest that a disruption of hydrogen bonds stabilizing the quinone-iron complex by Cu$\text{}^{2+}$ is the mechanism responsible for a new arrangement of the binding site of the non-heme iron leading to its more "tense" structure. Such a diamagnetic state of the non-heme iron induced by copper results in a magnetic decoupling of iron from the primary quinone acceptor. These results indicate that Cu does not cause removal of the non-heme iron from its binding site. The observed Cu$\text{}^{2+}$ action on the non-heme iron and cytochrome b$\text{}_{559}$ is similar to that previously observed forα-tocopherol quinone.
Źródło:: Acta Physica Polonica A; 2006, 109, 3; 237-247
0587-4246
1898-794X
Pojawia się w:: Acta Physica Polonica A
Dostawca treści:: Biblioteka Nauki

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