This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. The design work on the high-power stage of a receiver protector switch for 35 GHz is completed. We are integrating the ferrite switch with a fast, low-power, pin-diode switch that we recently acquired. We successfully tested a ferrite-based latching circulator intended for 35 GHz work. It is controlled by a home-built, fast, pulsed current driver. The switching speed is better than 20 ns, which is adequate for its use in FT-ESR. The repetition rate for this switch is 5 kHz, but we have not attempted to increase it further due to lack of a spare switch. The remaining work also includes minimizing electromagnetic interference from intense current pulses in its normal mode of operation as a part of the 35 GHz spectrometer. We routinely use 200 W limiters to handle 1-1.5 kW pulses of nanosecond duration for 8-18 GHz frequency range. For operating frequencies up to 18 GHz at higher peak power we recently procured passive receiver protectors rated to 1 kW for 1 ?s pulses. This would be adequate for nanosecond pulses of higher intensity. Their recovery time of 50 ns is adequate for low-temperature DQC work, but may be problematic for 2D-ELDOR for which dead-time should be under 30 ns. This would require a further effort to procure 20 ns ferrite switches and combine them with low-power diode limiters in order to achieve dead-time less than 25 ns. Ferrite switches for X and Ku bands with switching time under 20 ns are not available as standard products. What can be found is specified for larger switching energy than the 35 GHz switch, therefore we plan to obtain samples and study their switching performance.

National Institute of Health (NIH)
National Center for Research Resources (NCRR)
Biotechnology Resource Grants (P41)
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Cornell University
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Pratt, Ashley J; Shin, David S; Merz, Gregory E et al. (2014) Aggregation propensities of superoxide dismutase G93 hotspot mutants mirror ALS clinical phenotypes. Proc Natl Acad Sci U S A 111:E4568-76
Georgieva, Elka R; Borbat, Peter P; Ginter, Christopher et al. (2013) Conformational ensemble of the sodium-coupled aspartate transporter. Nat Struct Mol Biol 20:215-21
Airola, Michael V; Huh, Doowon; Sukomon, Nattakan et al. (2013) Architecture of the soluble receptor Aer2 indicates an in-line mechanism for PAS and HAMP domain signaling. J Mol Biol 425:886-901
Airola, Michael V; Sukomon, Nattakan; Samanta, Dipanjan et al. (2013) HAMP domain conformers that propagate opposite signals in bacterial chemoreceptors. PLoS Biol 11:e1001479
Sun, Yan; Zhang, Ziwei; Grigoryants, Vladimir M et al. (2012) The internal dynamics of mini c TAR DNA probed by electron paramagnetic resonance of nitroxide spin-labels at the lower stem, the loop, and the bulge. Biochemistry 51:8530-41
Yu, Renyuan Pony; Darmon, Jonathan M; Hoyt, Jordan M et al. (2012) High-Activity Iron Catalysts for the Hydrogenation of Hindered, Unfunctionalized Alkenes. ACS Catal 2:1760-1764
Dzikovski, Boris; Tipikin, Dmitriy; Freed, Jack (2012) Conformational distributions and hydrogen bonding in gel and frozen lipid bilayers: a high frequency spin-label ESR study. J Phys Chem B 116:6694-706
Gaffney, Betty J; Bradshaw, Miles D; Frausto, Stephen D et al. (2012) Locating a lipid at the portal to the lipoxygenase active site. Biophys J 103:2134-44
Maeda, Kiminori; Lodge, Matthew T J; Harmer, Jeffrey et al. (2012) Electron tunneling in lithium-ammonia solutions probed by frequency-dependent electron spin relaxation studies. J Am Chem Soc 134:9209-18
Georgieva, Elka R; Roy, Aritro S; Grigoryants, Vladimir M et al. (2012) Effect of freezing conditions on distances and their distributions derived from Double Electron Electron Resonance (DEER): a study of doubly-spin-labeled T4 lysozyme. J Magn Reson 216:69-77

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