Eliashberg theory for disordered superconductors. I. Tunneling into three-dimensional systems

1994 ◽  
Vol 93 (2) ◽  
pp. 163-172 ◽  
Author(s):  
Thorsten Höhn ◽  
Božidar Mitrović
1998 ◽  
Vol 12 (19) ◽  
pp. 763-773 ◽  
Author(s):  
Yong-Jihn Kim ◽  
K. J. Chang

We investigate the effect of weak localization on the transition temperatures of superconductors using Anderson's time-reversed scattered-state pairs, and show that disorder weakens electron–phonon interactions. With solving the BCS T c -equation, the calculated values for T c are in good agreement with experimental data for various two- and three-dimensional disordered superconductors. We find that the critical sheet resistance for the suppression of superconductivity in thin films does not satisfy the universal behavior but depends on sample, in good agreement with experiments.


1996 ◽  
Vol 166 (8) ◽  
pp. 904
Author(s):  
Vladimir N. Zverev ◽  
Vsevolod F. Gantmakher ◽  
V.M. Teplinskii

1996 ◽  
Vol 39 (8) ◽  
pp. 845-845
Author(s):  
Vladimir N Zverev ◽  
Vsevolod F Gantmakher ◽  
V M Teplinskii

1966 ◽  
Vol 25 ◽  
pp. 227-229 ◽  
Author(s):  
D. Brouwer

The paper presents a summary of the results obtained by C. J. Cohen and E. C. Hubbard, who established by numerical integration that a resonance relation exists between the orbits of Neptune and Pluto. The problem may be explored further by approximating the motion of Pluto by that of a particle with negligible mass in the three-dimensional (circular) restricted problem. The mass of Pluto and the eccentricity of Neptune's orbit are ignored in this approximation. Significant features of the problem appear to be the presence of two critical arguments and the possibility that the orbit may be related to a periodic orbit of the third kind.


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

The present knowledge of the three-dimensional structure of ribosomes is far too limited to enable a complete understanding of the various roles which ribosomes play in protein biosynthesis. The spatial arrangement of proteins and ribonuclec acids in ribosomes can be analysed in many ways. Determination of binding sites for individual proteins on ribonuclec acid and locations of the mutual positions of proteins on the ribosome using labeling with fluorescent dyes, cross-linking reagents, neutron-diffraction or antibodies against ribosomal proteins seem to be most successful approaches. Structure and function of ribosomes can be correlated be depleting the complete ribosomes of some proteins to the functionally inactive core and by subsequent partial reconstitution in order to regain active ribosomal particles.


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