Gramicidin A/gramicidin M heterodimer conductances were measured in planar lipid bilayers and found to form two distinguishable populations about halfway between the gramicidin A and gramicidin M homodimer conductances. This implies that the principle difference in the gramicidin A and gramicidin M transport free-energy profiles occurs at the channel center, where it would produce similar effects on the rate-limiting barrier for the two heterodimers. Kinetic analysis based on this and nearly all previously published homodimer conductance data for both gramicidin A and gramicidin M channels confirms this conclusion, indicating that the translocation step is approximately 100-fold slower in gramicidin M homodimers than in gramicidin A homodimers and that first- and second-ion exit-rate constants are higher by factors of 24 and 10, respectively. Assuming that the ratios of rate constants are related to the free-energy difference between gramicidin A and gramicidin M, we construct an effective ion-Trp free-energy interaction profile that has a minimum at the channel center.

Model-based iterative reconstruction reduces relative noise and improves CNR compared with ASIR and FBP at all kVp and mA settings, which were significantly greater at lower mA settings.

Synthesized monochromatic images between 40 and 60 keV maximize the magnitude of arterial enhancement and improve visualization of hepatic arterial anatomy at dual-energy MDCT angiography of the liver. Larger body sizes may counteract the benefits of using lower monochromatic energies.

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