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Abstract-In this paper, a novel transition design using vertical "coaxial transition" for coplanar waveguide (CPW-to-CPW) flip-chip interconnect is proposed and presented for the first time. The signal continuity is greatly improved since the coaxial-type transition provides more return current paths compared to the conventional transition in the flip-chip structure. The proposed coaxial transition structure shows a real coaxial property from the 3-D electromagnetic wave simulation results. The design rules for the coaxial transition are presented in detail with the key parameters of the coaxial transition structure discussed. For demonstration, the back-to-back flip-chip interconnect structures with the vertical coaxial transitions have been successfully fabricated and characterized. The demonstrated interconnect structure using the coaxial transition exhibits the return loss below 25 dB and the insertion loss within 0.4 dB from dc to 40 GHz. Furthermore, the measurement and simulation results show good agreement. The novel coaxial transition demonstrates excellent interconnect performance for flip-chip interconnects and shows great potential for flip-chip packaging applications at millimeter waves.
Mutations far from the center of chemical activity in dihydrofolate reductase (DHFR) can affect several steps in the catalytic cycle. Mutations at highly conserved positions and the distal distance of the catalytic center were designed, including single-point and double-point mutations. Upon ligand binding, the fluorescence of the intrinsic optical probe, tryptophan, decreases due to either fluorescence quenching or energy transfer. We demonstrated an optical approach in measuring the equilibrium dissociation constant for enzyme−cofactor, enzyme−substrate, and enzyme−product complexes in wildtype ecDHFR and each mutant. We propose that the effects of these distal mutations on ligand-binding affinity stem from the spatial steric hindrance, the disturbance on the hydrogen network, or the modification of the protein flexibility. The modified N-terminus tag in DHFR acts as a cap on the entrance of the substrate-binding cavity, squeezes the adenosine binding subdomain, and influences the binding of NADPH in some mutants. If the mutation positions are away from the N-terminus tag and the adenosine binding subdomain, the additive effects due to the Nterminus tag were not observed. In the double-mutant-cycle analysis, double mutations show nonadditive properties upon either cofactor or substrate binding. Also, in general, the first point mutation strongly affects the ligand binding compared to the second one.
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