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1.
Rev Sci Instrum ; 86(1): 013502, 2015 Jan.
Article in English | MEDLINE | ID: mdl-25638081

ABSTRACT

The paper concerns fast protons and neutrons from D-D fusion reactions in a Plasma-Focus-1000U facility. Measurements were performed with nuclear-track detectors arranged in "sandwiches" of an Al-foil and two PM-355 detectors separated by a polyethylene-plate. The Al-foil eliminated all primary deuterons, but was penetrable for fast fusion protons. The foil and first PM-355 detector were penetrable for fast neutrons, which were converted into recoil-protons in the polyethylene and recorded in the second PM-355 detector. The "sandwiches" were irradiated by discharges of comparable neutron-yields. Analyses of etched tracks and computer simulations of the fusion-products behavior in the detectors were performed.

2.
Rev Sci Instrum ; 82(3): 033505, 2011 Mar.
Article in English | MEDLINE | ID: mdl-21456735

ABSTRACT

We have developed and tested sensitive neutron detectors for neutron time-of-flight measurements in z-pinch and plasma focus experiments with neutron emission times in tens of nanoseconds and with neutron yields between 10(6) and 10(12) per one shot. The neutron detectors are composed of a BC-408 fast plastic scintillator and Hamamatsu H1949-51 photomultiplier tube (PMT). During the calibration procedure, a PMT delay was determined for various operating voltages. The temporal resolution of the neutron detector was measured for the most commonly used PMT voltage of 1.4 kV. At the PF-1000 plasma focus, a novel method of the acquisition of a pulse height distribution has been used. This pulse height analysis enabled to determine the single neutron sensitivity for various neutron energies and to calibrate the neutron detector for absolute neutron yields at about 2.45 MeV.

3.
Rev Sci Instrum ; 81(10): 10E312, 2010 Oct.
Article in English | MEDLINE | ID: mdl-21034011

ABSTRACT

Soft x-ray emission from a Mather-type plasma-focus device (PF-1000) operated at ∼400 kJ was measured. The high density and temperature plasma were generated by the discharge in the deuterium-argon gas mixture in the modified (high-current) plasma-focus configuration. A spherically bent mica crystal spectrograph viewing the axial output of the pinch region was used to measure the x-ray spectra. Spatially resolved spectra including the characteristic x-ray lines of highly ionized Ar and continua were recorded by means of an x-ray film. The x-ray emission of PF-1000 device was studied at different areas of the pinch.

4.
Acta Biochim Pol ; 48(4): 829-50, 2001.
Article in English | MEDLINE | ID: mdl-11995995

ABSTRACT

In recent years small G proteins have become an intensively studied group of regulatory GTP hydrolases involved in cell signaling. More than 100 small G proteins have been identified in eucaryotes from protozoan to human. The small G protein superfamily includes Ras, Rho Rab, Rac, Sarl/Arf and Ran homologs, which take part in numerous and diverse cellular processes, such as gene expression, cytoskeleton reorganization, microtubule organization, and vesicular and nuclear transport. These proteins share a common structural core, described as the G domain, and significant sequence similarity. In this paper we review the available data on G domain structure, together with a detailed analysis of the mechanism of action. We also present small G protein regulators: GTPase activating proteins that bind to a catalytic G domain and increase its low intrinsic hydrolase activity, GTPase dissociation inhibitors that stabilize the GDP-bound, inactive state of G proteins, and guanine nucleotide exchange factors that accelerate nucleotide exchange in response to cellular signals. Additionally, in this paper we describe some aspects of small G protein interactions with down-stream effectors.


Subject(s)
GTP-Binding Proteins/chemistry , Amino Acid Sequence , GTP Phosphohydrolases/metabolism , Humans , Hydrolysis , Models, Chemical , Models, Molecular , Molecular Sequence Data , Protein Conformation , Protein Structure, Tertiary , Sequence Homology, Amino Acid , Signal Transduction
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