scholarly journals Filaments and four ordered structures inside a neuron fire a thousand times faster than the membrane: theory and experiment

2021 ◽  
Vol 20 (4) ◽  
pp. 777-790
Author(s):  
Pushpendra Singh ◽  
Pathik Sahoo ◽  
Subrata Ghosh ◽  
Komal Saxena ◽  
Jhimli Sarkar Manna ◽  
...  
1993 ◽  
Vol 122 (1) ◽  
pp. 103-125 ◽  
Author(s):  
RAINER MELLIS† ◽  
WILLIAM N. GILL ◽  
GEORGES BELFORT

Author(s):  
A.-M. Ladhoff ◽  
B.J. Thiele ◽  
Ch. Coutelle ◽  
S. Rosenthal

The suggested precursor-product relationship between the nuclear pre-mRNA and the cytoplasmic mRNA has created increased interest also in the structure of these RNA species. Previously we have been published electron micrographs of individual pre-mRNA molecules from erythroid cells. An intersting observation was the appearance of a contour, probably corresponding to higher ordered structures, on one end of 10 % of the pre-mRNA molecules from erythroid rabbit bone marrow cells (Fig. 1A). A virtual similar contour was observed in molecules of 9S globin mRNA from rabbit reticulocytes (Fig. 1B). A structural transformation in a linear contour occurs if the RNA is heated for 10 min to 90°C in the presence of 80 % formamide. This structural transformation is reversible when the denatured RNA is precipitated and redissolved in 0.2 M ammonium acetate.


Author(s):  
U. Aebi ◽  
L.E. Buhle ◽  
W.E. Fowler

Many important supramolecular structures such as filaments, microtubules, virus capsids and certain membrane proteins and bacterial cell walls exist as ordered polymers or two-dimensional crystalline arrays in vivo. In several instances it has been possible to induce soluble proteins to form ordered polymers or two-dimensional crystalline arrays in vitro. In both cases a combination of electron microscopy of negatively stained specimens with analog or digital image processing techniques has proven extremely useful for elucidating the molecular and supramolecular organization of the constituent proteins. However from the reconstructed stain exclusion patterns it is often difficult to identify distinct stain excluding regions with specific protein subunits. To this end it has been demonstrated that in some cases this ambiguity can be resolved by a combination of stoichiometric labeling of the ordered structures with subunit-specific antibody fragments (e.g. Fab) and image processing of the electron micrographs recorded from labeled and unlabeled structures.


Author(s):  
Gertrude F. Rempfer

I became involved in electron optics in early 1945, when my husband Robert and I were hired by the Farrand Optical Company. My husband had a mathematics Ph.D.; my degree was in physics. My main responsibilities were connected with the development of an electrostatic electron microscope. Fortunately, my thesis research on thermionic and field emission, in the late 1930s under the direction of Professor Joseph E. Henderson at the University of Washington, provided a foundation for dealing with electron beams, high vacuum, and high voltage.At the Farrand Company my co-workers and I used an electron-optical bench to carry out an extensive series of tests on three-electrode electrostatic lenses, as a function of geometrical and voltage parameters. Our studies enabled us to select optimum designs for the lenses in the electron microscope. We early on discovered that, in general, electron lenses are not “thin” lenses, and that aberrations of focal point and aberrations of focal length are not the same. I found electron optics to be an intriguing blend of theory and experiment. A laboratory version of the electron microscope was built and tested, and a report was given at the December 1947 EMSA meeting. The micrograph in fig. 1 is one of several which were presented at the meeting. This micrograph also appeared on the cover of the January 1949 issue of Journal of Applied Physics. These were exciting times in electron microscopy; it seemed that almost everything that happened was new. Our opportunities to publish were limited to patents because Mr. Farrand envisaged a commercial instrument. Regrettably, a commercial version of our laboratory microscope was not produced.


Author(s):  
Weiping Liu ◽  
John W. Sedat ◽  
David A. Agard

Any real world object is three-dimensional. The principle of tomography, which reconstructs the 3-D structure of an object from its 2-D projections of different view angles has found application in many disciplines. Electron Microscopic (EM) tomography on non-ordered structures (e.g., subcellular structures in biology and non-crystalline structures in material science) has been exercised sporadically in the last twenty years or so. As vital as is the 3-D structural information and with no existing alternative 3-D imaging technique to compete in its high resolution range, the technique to date remains the kingdom of a brave few. Its tedious tasks have been preventing it from being a routine tool. One keyword in promoting its popularity is automation: The data collection has been automated in our lab, which can routinely yield a data set of over 100 projections in the matter of a few hours. Now the image processing part is also automated. Such automations finish the job easier, faster and better.


1978 ◽  
Vol 39 (12) ◽  
pp. 1355-1363 ◽  
Author(s):  
L.G. Caron ◽  
M. Miljak ◽  
D. Jerome

1986 ◽  
Vol 150 (10) ◽  
pp. 321
Author(s):  
V.L. Dunin-Barkovskii

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