Spontaneous regular structure amplification in strongly turbulent rotating fluids

1996 ◽  
Vol 53 (1) ◽  
pp. 493-497 ◽  
Author(s):  
E. A. Fedutenko
Author(s):  
Xiaorong Zhu ◽  
Richard McVeigh ◽  
Bijan K. Ghosh

A mutant of Bacillus licheniformis 749/C, NM 105 exhibits some notable properties, e.g., arrest of alkaline phosphatase secretion and overexpression and hypersecretion of RS protein. Although RS is known to be widely distributed in many microbes, it is rarely found, with a few exceptions, in laboratory cultures of microorganisms. RS protein is a structural protein and has the unusual properties to form aggregate. This characteristic may have been responsible for the self assembly of RS into regular tetragonal structures. Another uncommon characteristic of RS is that enhanced synthesis and secretion which occurs when the cells cease to grow. Assembled RS protein with a tetragonal structure is not seen inside cells at any stage of cell growth including cells in the stationary phase of growth. Gel electrophoresis of the culture supernatant shows a very large amount of RS protein in the stationary culture of the B. licheniformis. It seems, Therefore, that the RS protein is cotranslationally secreted and self assembled on the envelope surface.


2008 ◽  
Vol 17 (supp01) ◽  
pp. 304-317
Author(s):  
Y. M. ZHAO

In this paper we review regularities of low-lying states for many-body systems, in particular, atomic nuclei, under random interactions. We shall discuss the famous problem of spin zero ground state dominance, positive parity dominance, collective motion, odd-even staggering, average energies, etc., in the presence of random interactions.


1995 ◽  
Vol 74 (4) ◽  
pp. 530-533 ◽  
Author(s):  
Juan Millán-Rodríguez ◽  
Michael Bestehorn ◽  
Carlos Pérez-García ◽  
Rudolf Friedrich ◽  
Marc Neufeld
Keyword(s):  

1970 ◽  
Vol 16 (9) ◽  
pp. 883-887 ◽  
Author(s):  
R. G. E. Murray ◽  
Myrtle M. Hall ◽  
J. Marak

Sections of germinating spores of Bacillus polymyxa show that the primordial cell wall consists of a single layer. The intermediate layer and an outer rectangular array of macromolecules found on vegetative cells do not appear until the spore coats crack open about 60 min after initiation of germination. The initial areas of the new components appear in patches under the cracks in the coats. Within 10 min the wall is completed and takes on the profile seen in the vegetative cell. Negative staining and freeze-etching techniques show the regular structure to be identical with that previously shown for mature cells, although the subunits are more readily visible in negatively stained preparations.


1994 ◽  
Vol 107 (5) ◽  
pp. 1115-1129 ◽  
Author(s):  
C. Ferguson ◽  
A. Lakey ◽  
A. Hutchings ◽  
G.W. Butcher ◽  
K.R. Leonard ◽  
...  

Asynchronous insect flight muscles produce oscillatory contractions and can contract at high frequency because they are activated by stretch as well as by Ca2+. Stretch activation depends on the high stiffness of the fibres and the regular structure of the filament lattice. Cytoskeletal proteins may be important in stabilising the lattice. Two proteins, zeelin 1 (35 kDa) and zeelin 2 (23 kDa), have been isolated from the cytoskeletal fraction of Lethocerus flight muscle. Both zeelins have multiple isoforms of the same molecular mass and different charge. Zeelin 1 forms micelles and zeelin 2 forms filaments when renatured in low ionic strength solutions. Filaments of zeelin 2 are ribbons 10 nm wide and 3 nm thick. The position of zeelins in fibres from Lethocerus flight and leg muscle was determined by immunofluorescence and immunoelectron microscopy. Zeelin 1 is found in flight and leg fibres and zeelin 2 only in flight fibres. In flight myofibrils, both zeelins are in discrete regions of the A-band in each half sarcomere. Zeelin 1 is across the whole A-band in leg myofibrils. Zeelins are not in the Z-disc, as was thought previously, but migrate to the Z-disc in glycerinated fibres. Zeelins are associated with thick filaments and analysis of oblique sections showed that zeelin 1 is closer to the filament shaft than zeelin 2. The antibody labelling pattern is consistent with zeelin molecules associated with myosin near the end of the rod region. Alternatively, the position of zeelins may be determined by other A-band proteins. There are about 2.0 to 2.5 moles of myosin per mole of each zeelin. The function of these cytoskeletal proteins may be to maintain the ordered structure of the thick filament.


1994 ◽  
Vol 369 ◽  
Author(s):  
Steen Skaarup ◽  
L.M.W.K. Gunaratne ◽  
Keld West ◽  
Birgit Zachau-Christiansen

AbstractPolyaniline has been synthesized in propylene carbonate by galvanostatic electrochemical polymerization at current densities between 16 and 1000 μA/cm2. Earlier results for polypyrrole have shown that low and high current density films have different properties: The films synthesized at low current density have a higher conjugation length and a more regular structure. The corresponding effect in PANI has been investigated by cyclic voltammetry and UV/visible spectroscopy. Simultaneous measurement of cyclic voltammograms and the absorbtion of selected spectral lines is used because of the complex nature of the PANI system which involves several redox systems as well as forms differing in the degree of protonation and morphology.The main result is that the method of galvanostatic synthesis at low current densities (-16 μA/cm2) produces polyaniline polymers of different, more conjugated and more regular structure than those prepared at higher current densities. The standard method of in situ layer-by-layer polymerization of conducting polymers during cyclic voltammetry often results in uncontrolled and unmeasured current densities of 0.5-2 mA/cm2 which produces a film that probably has a less regular structure containing more deviations from ideality.


1968 ◽  
Vol 1 (2) ◽  
pp. 177-216 ◽  
Author(s):  
Jean Hanson

An intact living muscle has such a regular structure that it diffracts light or X-rays, thereby providing patterns that contain uniquely valuable information. Interpretation of these patterns is not straightforward, but is helped by light microscopy and electron microscopy, which can often provide similar though less reliable information. At all levels of complexity, from that of the fibrils to that of the molecules, structure in a muscle is orderly. No other natural cell assembly is so suited to study by the diffraction method, and the results obtained in recent years are an outstanding example of how this method can elucidate a biological problem. In contrast to protein crystallography, where the system studied is artificial, muscle can be examined in its natural state, during normal activity. The levels of structure explored as yet in muscle are above that of the atoms in the molecules. Such structure is more commonly investigated by electron microscopy, and the application of the diffraction method to living muscle has provided a valuable check on the preparative artifacts that worry the microscopist. The great complexity of a muscle, as compared with a protein crystal, and the fact that the system is only semi-crystalline, giving a much less detailed diffraction pattern, make the problems of interpretation especially difficult. But a great deal of useful information is available about other properties of muscle and its constituents, and the flourishing state of muscle biology at present is a major factor contributing to the successful application of the diffraction method.


2008 ◽  
Vol 47-50 ◽  
pp. 294-297 ◽  
Author(s):  
Xiu Wei Jia ◽  
Min Zhi Rong ◽  
Ming Qiu Zhang

A novel flame retardant polymethylsilsesquioxane (PMSQ) was successfully obtained via combination of non-hydrolytic and hydrolytic sol-gel routes. Chemical structure of the resultant PMSQ was determined by nuclear magnetic resonance spectroscopy, Fourier-transform infrared spectrometry and powder X-ray diffraction, respectively. All the measurements demonstrated that the product possessed regular structure with chain-to-chain width of 0.87nm and chain thickness of 0.40nm. Weight average molecular weight of PMSQ was measured to be 3.5×105 using gel permeation chromatography. Numerical simulations of the molecular structure suggested that PMSQ should exhibit cis-isotactic configuration and double helical conformation at undisturbed condition.


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