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The characterization of high electron mobility transistors using Shubnikov–de Haas oscillations and geometrical magnetoresistance measurements (1989)

Chang, Chian-Sern ; Fetterman, Harold R. ; Viswanathan, Chand R.

[S.l.] : American Institute of Physics (AIP)

Journal of Applied Physics 66 (1989), S. 928-936

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ISSN: 1089-7550

Source: AIP Digital Archive

Topics: Physics

Notes: Shubnikov–de Haas oscillations and geometrical magnetoresistance measurements are used to determine the two most important parameters, channel concentration and mobility, respectively, for high electron mobility transistors. To deduce useful data from measurements, the theory of the Shubnikov–de Haas oscillation for the two-dimensional electrons is derived and discussed in detail. The experimental data for the channel concentration as a function of gate voltage is used to check the accuracy of the charge-control law. We also derive a simple formula of the geometrical magnetoresistance to calculate the mobility for any aspect ratio. The concentration and mobility deduced from the Shubnikov–de Haas and geometrical magnetoresistance measurements give us insight on the nature and properties of the devices. The experimental data shows that the impurity scattering is the dominant mechanism for the low channel concentration. The maximum transconductance occurs at a compromise between the charge-control ability of the gate voltage and the channel mobility. Near the cutoff region the decrease of the conductivity is due to the decrease of both the channel concentration and the mobility.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1063/1.343522

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Binding studies of oxovanadium(V) with ovalbumins (OA) (1987)

Verma, S. R. ; Arora, J. P. S. ; Shankar, J. S. ; [et al.]

Springer

Water, air & soil pollution 36 (1987), S. 247-257

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ISSN: 1573-2932

Source: Springer Online Journal Archives 1860-2000

Topics: Energy, Environment Protection, Nuclear Power Engineering

Notes: Abstract The effect of protein oxovanadium(V) ion concentration and pH on the ratio of diffusion current (id/id0) was studied in vanadium(V) ovalbumin-S and denatured ovalbumin systems. In both the cases marked decrease in diffusion current was observed at the respective pH values, indicating that binding takes place with cationic groups of the proteins. The binding sites (n) were found to be pH dependent. The uniformity of logK and ΔG 0 value at all pH values indicated the involvement of same sites in interaction. Furthermore, the linear scatchard plots in both the systems supported the involvement of single class of independent sites in oxovanadium(V) anion interaction. The difference in binding sites (n) has been attributed to the folded structure of ovalbumin-S while unfolded one of denatured ovalbumin.