The Heliospheric Current Sheet: 3-Dimensional Structure and Solar Cycle Changes

Author(s):  
Edward J. Smith ◽  
J. A. Slavin ◽  
B. T. Thomas
2019 ◽  
Vol 47 (1) ◽  
pp. 85-87
Author(s):  
E.V. Maiewski ◽  
R.A. Kislov ◽  
H.V. Malova ◽  
O.V. Khabarova ◽  
V.Yu. Popov ◽  
...  

A stationary axisymmetric MHD model of the solar wind has been constructed, which allows us to study the spatial distribution of the magnetic field and plasma characteristics at radial distances from 20 to 400 radii of the Sun at almost all heliolatitudes. The model takes into account the changes in the magnetic field of the Sun during a quarter of the solar cycle, when the dominant dipole magnetic field is replaced by a quadrupole. Selfconsistent solutions for the magnetic and velocity fields, plasma concentration and current density of the solar wind depending on the phase of the solar cycle are obtained. It is shown that during the domination of the dipole magnetic component in the solar wind heliospheric current sheet (HCS) is located in the equatorial plane, which is a part of the system of radial and transverse currents, symmetrical in the northern and southern hemispheres. As the relative contribution of the quadrupole component to the total magnetic field increases, the shape of the HCS becomes conical; the angle of the cone gradually decreases, so that the current sheet moves entirely to one of the hemispheres. At the same time, at high latitudes of the opposite hemisphere, a second conical HCS arises, the angle of which increases. When the quadrupole field becomes dominant (at maximum solar activity), both HCS lie on conical surfaces inclined at an angle of 35 degrees to the equator. The model describes the transition from the fast solar wind at high latitudes to the slow solar wind at low latitudes: a relatively gentle transition in the period of low solar activity gives way to more drastic when high solar activity. The model also predicts an increase in the steepness of the profiles of the main characteristics of the solar wind with an increase in the radial distance from the Sun. Comparison of the obtained dependences with the available observational data is discussed.


1994 ◽  
Vol 144 ◽  
pp. 83-89 ◽  
Author(s):  
E. W. Cliver ◽  
O. C. St. Cyr ◽  
R. A. Howard ◽  
P. S. McIntosh

AbstractWe obtained Carrington-rotation-averaged daily rates of coronal mass ejections (CMEs), corrected for duty cycle, for the period 1979-1989. The 27-day averages of CME rate and sunspot number are correlated over this 11-yr period, although significant discrepancies can occur for any given rotation. The baseline CME rate exhibited quasi-discontinuities in 1982 (decrease) and 1988 (increase) when the “tilt angle” of the heliospheric current sheet passed through values of ∼ 50°. We suggest that these quasi-discontinuities are related to the dynamics of the belts of polar crown filaments that reside at ∼ 50° north and south of the equator during solar minimum and move poleward during the rise phase of the solar cycle.


2001 ◽  
Vol 376 (1) ◽  
pp. 288-291 ◽  
Author(s):  
P. L. Israelevich ◽  
T. I. Gombosi ◽  
A. I. Ershkovich ◽  
K. C. Hansen ◽  
C. P. T. Groth ◽  
...  

Author(s):  
Robert Glaeser ◽  
Thomas Bauer ◽  
David Grano

In transmission electron microscopy, the 3-dimensional structure of an object is usually obtained in one of two ways. For objects which can be included in one specimen, as for example with elements included in freeze- dried whole mounts and examined with a high voltage microscope, stereo pairs can be obtained which exhibit the 3-D structure of the element. For objects which can not be included in one specimen, the 3-D shape is obtained by reconstruction from serial sections. However, without stereo imagery, only detail which remains constant within the thickness of the section can be used in the reconstruction; consequently, the choice is between a low resolution reconstruction using a few thick sections and a better resolution reconstruction using many thin sections, generally a tedious chore. This paper describes an approach to 3-D reconstruction which uses stereo images of serial thick sections to reconstruct an object including detail which changes within the depth of an individual thick section.


Author(s):  
A. Engel ◽  
A. Holzenburg ◽  
K. Stauffer ◽  
J. Rosenbusch ◽  
U. Aebi

Reconstitution of solubilized and purified membrane proteins in the presence of phospholipids into vesicles allows their functions to be studied by simple bulk measurements (e.g. diffusion of differently sized solutes) or by conductance measurements after transformation into planar membranes. On the other hand, reconstitution into regular protein-lipid arrays, usually forming at a specific lipid-to-protein ratio, provides the basis for determining the 3-dimensional structure of membrane proteins employing the tools of electron crystallography.To refine reconstitution conditions for reproducibly inducing formation of large and highly ordered protein-lipid membranes that are suitable for both electron crystallography and patch clamping experiments aimed at their functional characterization, we built a flow-dialysis device that allows precise control of temperature and flow-rate (Fig. 1). The flow rate is generated by a peristaltic pump and can be adjusted from 1 to 500 ml/h. The dialysis buffer is brought to a preselected temperature during its travel through a meandering path before it enters the dialysis reservoir. A Z-80 based computer controls a Peltier element allowing the temperature profile to be programmed as function of time.


Author(s):  
D.P. Bazett-Jones ◽  
F.P. Ottensmeyer

It has been shown for some time that it is possible to obtain images of small unstained proteins, with a resolution of approximately 5Å using dark field electron microscopy (1,2). Applying this technique, we have observed a uniformity in size and shape of the 2-dimensional images of pure specimens of fish protamines (salmon, herring (clupeine, Y-l) and rainbow trout (Salmo irideus)). On the basis of these images, a model for the 3-dimensional structure of the fish protamines has been proposed (2).The known amino acid sequences of fish protamines show stretches of positively charged arginines, separated by regions of neutral amino acids (3). The proposed model for protamine structure (2) consists of an irregular, right-handed helix with the segments of adjacent arginines forming the loops of the coil.


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