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Challenges of ERAU’s First Suborbital Flight Aboard Blue Origin’s New Shepard M7 for the Cell Research Experiment In Microgravity (CRExIM)

% duplicate packets in the data and a 0.3% dropped packet count as provided by the NanoRacks team to maximize the data collection for the next mission. The data observed in Figure 5 were provided by Blue Origin at 100 Hz and shows evidence of some very short shock events at CC separation ( Figure 5d), drogue chute deployment ( Figure 5g), and main chute deployment ( Figure 5h). These pulses are only a single data point wide, suggesting pulse durations <100 ms. These pulses were the result of the reaction control system when firing their thrusters right after capsule

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Musculoskeletal Outcomes from Chronic High-Speed High-Impact Resistive Exercise

; greater (p<0.05) than the other treatment means for that velocity. PT, peak torque; SEM, standard error of the mean. Table 3 Knee extensor TTPT (mean ± SEM in seconds) results. Velocity (rad./second) Left leg Right leg Pre-intervention Post-intervention Pre-intervention Post-intervention 0 2.06±0.20 2.35±0.24 2.03±0.25 2.04±0.33 1.62 0.37±0.02 0.39±0.03 0.37±0.04 0.33±0.02 4.86 0.19±0.02 0.18±0.02 0.18±0.02 0.19±0.02 SEM, standard error of the mean; TTPT, time to peak torque

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Impact of g-Load Shift on Temporal Expression Pattern of Apoptosis-linked Proteins in the Rat Mammary Gland

) . Effect of HG on Temporal Distribution of VDR Protein The time-trend quantitative profile of mammary gland lobular VDR in SC and HG rats is depicted in Figure 2e and f . VDR protein concentration declined by about 50% (p<0.001) in SC animals during the transition from G20 (3.6±0.24 px) to P1 (1.8±0.05 px). Subsequently, the VDR levels increased approximately fivefold (p<0.001) at P3 (10.8±0.52 px) versus P1 levels in the SC group ( Fig. 2e) . On the other hand, the HG-G20 (7.03±0.28 px) rats had about 300% (p<0.001) more VDR expressed than their P1 (2.09±0.11 px

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Effect of macromolecular mass transport in microgravity protein crystallization

reaction was incubated for 1 h at room temperature with continuous stirring. The labeled tetramer was separated from free dye using a Sephadex® G-25 prepacked gel filtration column. The column was first equilibrated with PBS buffer and then loaded with a reaction mixture and eluted with PBS buffer solution. Labeling degree (DOL) of tetramer was calculated using following calculations: (1) Protein   concentration   ( M ) = [ A 280 − ( CF × A 494 ) ] × dilution   factor ε ( protein ) $$ \text

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Investigation of Murine T-Cells and Cancer Cells under Thermal Stressors and 2D Slow Rotating System Effects as a Testbed for Suborbital Flights

and 3 g during ascent for about 2.5 min, between 1 g and 5 g during descent for nearly 1.5 min, and some instances with accelerations between 2 g and 3 g during parachute recovery for almost 30 sec, total time of about 5 min. Then they were either placed in 2, 5, or 15 mL tubes with and without cytokines and maintained in water baths at the following temperatures: 37℃, 30℃, 34℃, and 40℃ for various time points. Cells were also exposed to other thermal baths at 10℃ and 20℃ to account for extreme temperature variations during launch conditions as we will refer to

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