New Aspects of Quasi-Kondo Physics: Two-Level Kondo and Strongly Coupled Local Electron–Phonon Systems

2005 ◽  
Vol 74 (1) ◽  
pp. 49-58 ◽  
Author(s):  
Satoshi Yotsuhashi ◽  
Masatsugu Kojima ◽  
Hiroaki Kusunose ◽  
Kazumasa Miyake
Keyword(s):  
Local Electron ◽  
Strongly Coupled ◽  
Kondo Physics

Lithography below 100 nm

1983 ◽  
Vol 41 ◽  
pp. 96-99
Author(s):  
L. D. Jackel
Keyword(s):  
Spatial Distribution ◽  
Electron Beam ◽  
Electron Scattering ◽  
Electron Beam Lithography ◽  
Substrate Material ◽  
Local Electron ◽  
Electron Dose ◽  
Positive Resist ◽  
Exposure Process

Most production electron beam lithography systems can pattern minimum features a few tenths of a micron across. Linewidth in these systems is usually limited by the quality of the exposing beam and by electron scattering in the resist and substrate. By using a smaller spot along with exposure techniques that minimize scattering and its effects, laboratory e-beam lithography systems can now make features hundredths of a micron wide on standard substrate material. This talk will outline sane of these high- resolution e-beam lithography techniques.We first consider parameters of the exposure process that limit resolution in organic resists. For concreteness suppose that we have a “positive” resist in which exposing electrons break bonds in the resist molecules thus increasing the exposed resist's solubility in a developer. Ihe attainable resolution is obviously limited by the overall width of the exposing beam, but the spatial distribution of the beam intensity, the beam “profile” , also contributes to the resolution. Depending on the local electron dose, more or less resist bonds are broken resulting in slower or faster dissolution in the developer.

Strongly coupled nonneutral plasmas : Equilibrium and relaxation in two-component plasmas in Penning-Malmberg trap

2000 ◽  
Vol 10 (PR5) ◽  
pp. Pr5-271-Pr5-274
Author(s):  
H. Totsuji ◽  
K. Tsuruta ◽  
C. Totsuji ◽  
K. Nakano ◽  
T. Kishimoto ◽  
...  
Keyword(s):  
Strongly Coupled ◽  
Nonneutral Plasmas ◽  
Two Component

Analysis of Operation Margin and Read Speed in 6T- and 8T-SRAM with Local Electron Injected Asymmetric Pass Gate Transistor

2012 ◽  
Vol E95-C (4) ◽  
pp. 564-571 ◽  
Author(s):  
Kousuke MIYAJI ◽  
Kentaro HONDA ◽  
Shuhei TANAKAMARU ◽  
Shinji MIYANO ◽  
Ken TAKEUCHI
Keyword(s):  
Local Electron

Strongly Coupled Redox-Linked Conformational Switching at the Active Site of the Non-Heme Iron-Dependent Dioxygenase, TauD

2019 ◽  
Author(s):  
Christopher John ◽  
Greg M. Swain ◽  
Robert P. Hausinger ◽  
Denis A. Proshlyakov
Keyword(s):  
Active Site ◽  
Structural Model ◽  
Heme Iron ◽  
Chemical Transformations ◽  
Experimental Conditions ◽  
Strongly Coupled ◽  
Non Heme Iron ◽  
Reversible Redox ◽  
Wide Range ◽  
Complex Structural

2-Oxoglutarate (2OG)-dependent dioxygenases catalyze C-H activation while performing a wide range of chemical transformations. In contrast to their heme analogues, non-heme iron centers afford greater structural flexibility with important implications for their diverse catalytic mechanisms. We characterize an <i>in situ</i> structural model of the putative transient ferric intermediate of 2OG:taurine dioxygenase (TauD) by using a combination of spectroelectrochemical and semi-empirical computational methods, demonstrating that the Fe (III/II) transition involves a substantial, fully reversible, redox-linked conformational change at the active site. This rearrangement alters the apparent redox potential of the active site between -127 mV for reduction of the ferric state and 171 mV for oxidation of the ferrous state of the 2OG-Fe-TauD complex. Structural perturbations exhibit limited sensitivity to mediator concentrations and potential pulse duration. Similar changes were observed in the Fe-TauD and taurine-2OG-Fe-TauD complexes, thus attributing the reorganization to the protein moiety rather than the cosubstrates. Redox difference infrared spectra indicate a reorganization of the protein backbone in addition to the involvement of carboxylate and histidine ligands. Quantitative modeling of the transient redox response using two alternative reaction schemes across a variety of experimental conditions strongly supports the proposal for intrinsic protein reorganization as the origin of the experimental observations.

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