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TCAD simulation of tunneling leakage current in CaF2/Si(111) MIS structures
Yu.Yu. Illarionov,M.I. Vexler,M. Karner,S.E. Tyaginov,J. Cervenka,T. Grasser 한국물리학회 2015 Current Applied Physics Vol.15 No.2
We introduce a simulation technique suitable to model the tunneling leakage current in the metal(- polySi)/CaF2/Si(111) MIS structures using TCAD simulators Minimos-NT and ViennaSHE. The simulations are performed using the real physical parameters of the CaF2/Si tunnel barrier. The results obtained for the case of near-equilibrium carrier transport are in a good agreement with experimental data and also with the simulation results yielded by our reference physical model. The obtained non-equilibrium hotelectron tunnel leakages in the hypothetical transistors with CaF2 as a gate dielectric are comparable to those in the structures with silicon dioxide. Being an important step forward for the device application of calcium fluorite, this work opens the possibility of simulating the characteristics of different siliconbased systems with crystalline insulators.
Ligand Binding Properties of the N-Terminal Domain of Riboflavin Synthase from Escherichia coli
( Chan Yong Lee ),( Boris Illarionov ),( Young Eun Woo ),( Kristina Kemter ),( Ryu Ryun Kim ),( Sabine Eberhardt ),( Mark Cushman ),( Wolfgang Eisenreich ),( Markus Fischer ),( Adelbert Bacher ) 생화학분자생물학회 2007 BMB Reports Vol.40 No.2
Ligand Binding Properties of the N-Terminal Domain of Riboflavin Synthase from Escherichia coli
Lee, Chan-Yong,Illarionov, Boris,Woo, Young-Eun,Kemter, Kristina,Kim, Ryu-Ryun,Eberhardt, Sabine,Cushman, Mark,Eisenreich, Wolfgang,Fischer, Markus,Bacher, Adelbert Korean Society for Biochemistry and Molecular Biol 2007 Journal of biochemistry and molecular biology Vol.40 No.2
Riboflavin synthase from Escherichia coli is a homotrimer of 23.4 kDa subunits and catalyzes the formation of one molecule each of riboflavin and 5-amino-6-ribitylamino- 2,4(1H,3H)-pyrimidinedione by the transfer of a 4-carbon moiety between two molecules of the substrate, 6,7- dimethyl-8-ribityllumazine. Each subunit comprises two closely similar folding domains. Recombinant expression of the N-terminal domain is known to provide a $C_2$-symmetric homodimer. In this study, the binding properties of wild type as well as two mutated proteins of N-terminal domain of riboflavin synthase with various ligands were tested. The replacement of the amino acid residue A43, located in the second shell of riboflavin synthase active center, in the recombinant N-terminal domain dimer reduces the affinity for 6,7-dimethyl-8-ribityllumazine. The mutation of the amino acid residue C48 forming part of activity cavity of the enzyme causes significant $^{19}F$ NMR chemical shift modulation of trifluoromethyl derivatives of 6,7-dimethyl-8-ribityllumazine in complex with the protein, while substitution of A43 results in smaller chemical shift changes.