Mutual orientation of crystallites in process of corundum formation in supercritical water fluid

2011 ◽  
Vol 66 (5) ◽  
pp. 290-298 ◽  
Author(s):  
A. V. Maryashkin ◽  
Yu. D. Ivakin ◽  
M. N. Danchevskaya ◽  
G. P. Murav’eva ◽  
M. N. Kirikova

2004 ◽  
Vol 16 (14) ◽  
pp. S1215-S1221 ◽  
Author(s):  
G P Panasyuk ◽  
M N Danchevskaya ◽  
V N Belan ◽  
I L Voroshilov ◽  
Yu D Ivakin

2015 ◽  
Vol 9 (7) ◽  
pp. 1082-1094 ◽  
Author(s):  
Yu. D. Ivakin ◽  
M. N. Danchevskaya ◽  
G. P. Muravieva

Author(s):  
R Zakieva ◽  
B Affane ◽  
A Nosova ◽  
A Okruzhnov ◽  
N Bashkirtseva

2013 ◽  
Vol 49 (9) ◽  
pp. 899-903 ◽  
Author(s):  
G. P. Panasyuk ◽  
I. V. Luchkov ◽  
I. V. Kozerozhets ◽  
D. G. Shabalin ◽  
V. N. Belan

Author(s):  
M. Boublik ◽  
N. Robakis ◽  
W. Hellmann ◽  
F. Jenkins

Ribosomes are ribonucleoprotein particles which process the genetic information coded in mRNA into protein synthesis. The analogy in function and composition of ribosomes from various sources, both prokaryotic and eukaryo-tic, imply a structural similarity. At present, high resolution electron microscopy is the most direct technique with a potential to resolve the extent of the structural homology of ribosomal particles at a macromolecular level. The structure of ribosomes is highly complex as a result of the large number of their constituents. In general, 80S eukaryotic monosomes consist of two uneven subunits - large (60S) and small (40S) - accomodating four different RNAs and approximately 80 different proteins. Mutual orientation of both subunits on the monosome is of particular interest because it determines the interface, the supposed site of interactions of ribosomes with other macro-molecules involved in peptide bond formation. Since entrapping of the contrasting solution (0.5% aqueous uranyl acetate) obscures all structural details in the interface, information on its architecture is limited to an indirect reconstruction based on the established 3-D structure of both sub-units and their mutual position after association.


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