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J Tschanz - One of the best experts on this subject based on the ideXlab platform.
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serial link bus a low power on chip bus architecture
IEEE Transactions on Circuits and Systems, 2009Co-Authors: Maged Ghoneima, Yehea Ismail, Muhammad M Khellah, J TschanzAbstract:As technology scales, the shrinking wire width increases the interconnect resistivity, while the decreasing interconnect spacing significantly increases the coupling capacitance. This paper proposes reducing the number of bus lines of the conventional parallel-line bus (PLB) architecture by multiplexing each m-bits onto a single line. This bus architecture, the serial-link bus (SLB), transforms an n-bit conventional PLB into an n/m-line (serial link) bus. The advantage of SLBs is that they have fewer lines, and if the bus width is kept the same, SLBs will have a larger line pitch. Increasing the line width has a twofold reduction effect on the line resistance; as the resistivity of sub-100 nm wires drops significantly, the line width increases. Also, increasing the line width and spacing reduces the coupling capacitance between adjacent lines, but increases the line-to-ground capacitance. Thus, an optimum degree of multiplexing m opt and an optimum width to pitch ratio etaopt exist, which minimizes the bus energy dissipation and maximizes the bus throughput per unit area. The optimum degree of multiplexing and optimum width-to-pitch ratio for maximum throughput per unit area and minimum energy dissipation for the 25-130-nm technologies was determined in this paper. Also, an encoding technique was proposed and implemented to reduce the switch activity penalty due to serialization. HSPICE simulations show that for the same throughput per unit area as conventional parallel-line data buses, the SLB architecture reduces the energy dissipation by up to 31% for a 64-bit bus implemented in an Intermediate Metal layer of a 50-nm technology, and a reduction of 53% is projected for a 25-nm technology.
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serial link bus a low power on chip bus architecture
International Conference on Computer Aided Design, 2005Co-Authors: Maged Ghoneima, Yehea Ismail, Muhammad M Khellah, J TschanzAbstract:As technology scales, the shrinking wire width increases the interconnect resistivity, while the decreasing interconnect spacing significantly increases the coupling capacitance. This paper proposes reducing the number of bus lines of the conventional parallel-line bus CB architecture by multiplexing each m-bits onto a single line. This bus architecture, the serial-link bus SLB, transforms an n-bit conventional parallel-line bus into an n/m-line (serial-link) bus. The advantage of serial-link buses is that they have fewer lines, and if the bus width is kept the same, serial- link buses will have larger line width and spacing. Increasing the line width has a twofold reduction effect on the line resistance, as the resistivity of sub-100 nm wires significantly drops as the line width increases. Also, increasing the line width and spacing reduces the coupling capacitance between adjacent lines, but increases the line-to-ground capacitance. Thus, an optimum degree of multiplexing m exists that minimizes the bus energy dissipation and maximizes the bus throughput per-unit area. The optimum degree of multiplexing for maximum throughput-per- unit-area and for minimum energy dissipation for the 25-130 nm technologies was determined in this paper. HSPICE simulations show that; for the same throughput-per-unit-area as conventional parallel-line buses, the serial-link bus architecture reduces the energy dissipation by up to 31.42% for a 64-bit bus implemented in an Intermediate Metal layer of a 50 nm technology and a reduction of 52.7% is projected for the 25 nm technology.
Liezelle C Lopez - One of the best experts on this subject based on the ideXlab platform.
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characterization and effect of Metal ions on the formation of the thermus thermophilus sco mixed disulfide Intermediate Metal binding and mdi formation of t thermophilus sco
Protein Science, 2018Co-Authors: Liezelle C Lopez, Nikita Mukhitov, Lindsey D Handley, Cristina S Hamme, Cristina R Hofman, Lindsay Euers, Jennifer R MckinneyAbstract:: The Sco protein from Thermus thermophilus has previously been shown to perform a disulfide bond reduction in the CuA protein from T. thermophilus, which is a soluble protein engineered from subunit II of cytochrome ba 3 oxidase that lacks the transmembrane helix. The native cysteines on TtSco and TtCuA were mutated to serine residues to probe the reactivities of the individual cysteines. Conjugation of TNB to the remaining cysteine in TtCuA and subsequent release upon incubation with the complementary TtSco protein demonstrated the formation of the mixed disulfide Intermediate. The cysteine of TtSco that attacks the disulfide bond in the target TtCuA protein was determined to be TtSco Cysteine 49. This cysteine is likely more reactive than Cysteine 53 due to a higher degree of solvent exposure. Removal of the Metal binding histidine, His 139, does not change MDI formation. However, altering the arginine adjacent to the reactive cysteine in Sco (Arginine 48) does alter the formation of the MDI. Binding of Cu2+ or Cu+ to TtSco prior to reaction with TtCuA was found to preclude formation of the mixed disulfide Intermediate. These results shed light on a mechanism of disulfide bond reduction by the TtSco protein and may point to a possible role of Metal binding in regulating the activity. IMPORTANCE: The function of Sco is at the center of many studies. The disulfide bond reduction in CuA by Sco is investigated herein and the effect of Metal ions on the ability to reduce and form a mixed disulfide Intermediate are also probed.
Jennifer R Mckinney - One of the best experts on this subject based on the ideXlab platform.
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characterization and effect of Metal ions on the formation of the thermus thermophilus sco mixed disulfide Intermediate Metal binding and mdi formation of t thermophilus sco
Protein Science, 2018Co-Authors: Liezelle C Lopez, Nikita Mukhitov, Lindsey D Handley, Cristina S Hamme, Cristina R Hofman, Lindsay Euers, Jennifer R MckinneyAbstract:: The Sco protein from Thermus thermophilus has previously been shown to perform a disulfide bond reduction in the CuA protein from T. thermophilus, which is a soluble protein engineered from subunit II of cytochrome ba 3 oxidase that lacks the transmembrane helix. The native cysteines on TtSco and TtCuA were mutated to serine residues to probe the reactivities of the individual cysteines. Conjugation of TNB to the remaining cysteine in TtCuA and subsequent release upon incubation with the complementary TtSco protein demonstrated the formation of the mixed disulfide Intermediate. The cysteine of TtSco that attacks the disulfide bond in the target TtCuA protein was determined to be TtSco Cysteine 49. This cysteine is likely more reactive than Cysteine 53 due to a higher degree of solvent exposure. Removal of the Metal binding histidine, His 139, does not change MDI formation. However, altering the arginine adjacent to the reactive cysteine in Sco (Arginine 48) does alter the formation of the MDI. Binding of Cu2+ or Cu+ to TtSco prior to reaction with TtCuA was found to preclude formation of the mixed disulfide Intermediate. These results shed light on a mechanism of disulfide bond reduction by the TtSco protein and may point to a possible role of Metal binding in regulating the activity. IMPORTANCE: The function of Sco is at the center of many studies. The disulfide bond reduction in CuA by Sco is investigated herein and the effect of Metal ions on the ability to reduce and form a mixed disulfide Intermediate are also probed.
W Freude - One of the best experts on this subject based on the ideXlab platform.
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surface plasmon polariton absorption modulator
Optics Express, 2011Co-Authors: Argishti Melikyan, N Lindenmann, Stefan Walheim, Philipp M Leufke, S Ulrich, P Vincze, Horst Hahn, Th Schimmel, C Koos, W FreudeAbstract:An electrically controlled ultra-compact surface plasmon polariton absorption modulator (SPPAM) is proposed. The device can be as small as a few micrometers depending on the required extinction ratio and the acceptable loss. The device allows for operation far beyond 100 Gbit / s, being only limited by RC time constants. The absorption modulator comprises a stack of Metal / insulator / Metal-oxide / Metal layers, which support a strongly confined asymmetric surface plasmon polariton (SPP) in the 1.55 μm telecommunication wavelength window. Absorption modulation is achieved by electrically modulating the free carrier density in the Intermediate Metal-oxide layer. The concept is supported by proof-of-principle experiments.
Lindsay Euers - One of the best experts on this subject based on the ideXlab platform.
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characterization and effect of Metal ions on the formation of the thermus thermophilus sco mixed disulfide Intermediate Metal binding and mdi formation of t thermophilus sco
Protein Science, 2018Co-Authors: Liezelle C Lopez, Nikita Mukhitov, Lindsey D Handley, Cristina S Hamme, Cristina R Hofman, Lindsay Euers, Jennifer R MckinneyAbstract:: The Sco protein from Thermus thermophilus has previously been shown to perform a disulfide bond reduction in the CuA protein from T. thermophilus, which is a soluble protein engineered from subunit II of cytochrome ba 3 oxidase that lacks the transmembrane helix. The native cysteines on TtSco and TtCuA were mutated to serine residues to probe the reactivities of the individual cysteines. Conjugation of TNB to the remaining cysteine in TtCuA and subsequent release upon incubation with the complementary TtSco protein demonstrated the formation of the mixed disulfide Intermediate. The cysteine of TtSco that attacks the disulfide bond in the target TtCuA protein was determined to be TtSco Cysteine 49. This cysteine is likely more reactive than Cysteine 53 due to a higher degree of solvent exposure. Removal of the Metal binding histidine, His 139, does not change MDI formation. However, altering the arginine adjacent to the reactive cysteine in Sco (Arginine 48) does alter the formation of the MDI. Binding of Cu2+ or Cu+ to TtSco prior to reaction with TtCuA was found to preclude formation of the mixed disulfide Intermediate. These results shed light on a mechanism of disulfide bond reduction by the TtSco protein and may point to a possible role of Metal binding in regulating the activity. IMPORTANCE: The function of Sco is at the center of many studies. The disulfide bond reduction in CuA by Sco is investigated herein and the effect of Metal ions on the ability to reduce and form a mixed disulfide Intermediate are also probed.