|
| |
|
| |
|
| |
|
|
Surface-related 2D conductivity of nanocrystalline diamond in-plane nanowires
Rezek, Bohuslav ; Babchenko, Oleg ; Vetushka, Aliaksi ; Verveniotis, Elisseos ; Ledinský, Martin ; Fejfar, Antonín ; Kromka, Alexander
Diamond is an attractive material for nanoelectronics, biological interfaces and electrical transducers. Small device dimensions are highly demanded for higher sensitivity, parallelism, remote sensing and reduced costs. Recently we have demonstrated that directly grown nanocrystalline diamond micro-channels (down to 5 um widths) are feasible and fully operational as field-effect transistors using H-terminated surface conductivity.
|
|
| |
|
| |
|
|
Synthesis, structure, and opto-electronic properties of organic dies on diamond
Rezek, Bohuslav ; Čermák, Jan ; Ukraintsev, Egor ; Hubík, Pavel ; Mareš, Jiří J. ; Ledinský, Martin ; Fejfar, Antonín ; Kočka, Jan ; Kromka, Alexander
We prepare a thin-film heterojunction of polypyrrole (Ppy) on hydrogen-terminated diamond by electro-polymerization from solution. We combine advanced scanning techniques (AFM, KFM, micro-Raman) to characterize microscopic structural, chemical, and opto-electronic properties of such system.
|
|
| |
|
|
Structural analysis of extrinsic proteins from the oxygen-evolving complex of photosystem II from higher plants
KOHOUTOVÁ, Jaroslava
All life on earth depends mainly on the presence of oxygen. Largest producers of oxygen are green plants, cyanobacteria and algae. Oxygen is released from the oxygenevolving complex of photosystem II during photosynthesis and it is used in cellular respiration of all life complexes. The oxygen-evolving complex of photosystem II has the same function in each photosynthetic organism, but it has a different composition and organization of extrinsic proteins; only PsbO protein is ubiquitous in all known oxyphototrophs. Until now only low resolution electron microscopy structural models of plant PSII and crystal structures of cyanobacterial PSII are available. Higher plant extrinsic proteins (PsbP, PsbQ and PsbR) are structurally unrelated, non-homologues to the cyanobacterial extrinsic proteins (PsbO, PsbU and PsbV) and this is the reason why it is not possible to predict arrangement of these proteins on the lumenal site of higher plant PSII. Recently, models differ mainly in the structure of the oxygen-evolving complex, which could be resolved by determination of the exact binding sites for extrinsic proteins. An other question evolves: if the difference in the oxygen-evolving complex composition is the result of evolution or adaptation of photosynthetic organisms to their environment. Structural knowledge of extrinsic proteins that could help to resolve the location and subsequently the function of extrinsic proteins is still incomplete. From this case,structural analysis, interactions and probably arrangement of proteins PsbP and PsbQ was studied and is described in detail in this thesis.
|
|
|
Primary electron scattering on biological specimen embedding resins at low voltage transmission electron microscope LV EM 5
BÍLÝ, Tomáš
This master thesis deals with researching the structure of embedding resin in the Low-Voltage Transmission Electron Microscope (LV TEM). Further, it focuses on researching the surface morphology by the Atomic Force Microscope (AFM) and by the Scanning Electron Microscope (SEM). The principle of each of the microscopes is explained ? the contrast formation and construction of the LV TEM in particular. In the conclusion the evaluation of the effect of the surface structure of the embedding resin on the image contrast in the LV TEM and the analysis of the minimalization of its effect on the final image is given.
|
guest ::
