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We present a new approach to the problem of optimal control of solar sails for low-thrust trajectory optimization. The objective was to find the required control torque magnitudes in order to steer a solar sail in interplanetary space. A new steering strategy, controlling the solar sail with generic torques applied about the spacecraft body axes, is integrated into the existing low-thrust trajectory optimization software InTrance. This software combines artificial neural networks and evolutionary algorithms to find steering strategies close to the global optimum without an initial guess. Furthermore, we implement a three rotational degree-of-freedom rigid-body attitude dynamics model to represent the solar sail in space. Two interplanetary transfers to Mars and Neptune are chosen to represent typical future solar sail mission scenarios. The results found with the new steering strategy are compared to the existing reference trajectories without attitude dynamics. The resulting control torques required to accomplish the missions are investigated, as they pose the primary requirements to a real on-board attitude control system.
Background
Minor changes in protein structure induced by small organic and inorganic molecules can result in significant metabolic effects. The effects can be even more profound if the molecular players are chemically active and present in the cell in considerable amounts. The aim of our study was to investigate effects of a nitric oxide donor (spermine NONOate), ATP and sodium/potassium environment on the dynamics of thermal unfolding of human hemoglobin (Hb). The effect of these molecules was examined by means of circular dichroism spectrometry (CD) in the temperature range between 25°C and 70°C. The alpha-helical content of buffered hemoglobin samples (0.1 mg/ml) was estimated via ellipticity change measurements at a heating rate of 1°C/min.
Results
Major results were:
1) spermine NONOate persistently decreased the hemoglobin unfolding temperature T u irrespectively of the Na + /K + environment,
2) ATP instead increased the unfolding temperature by 3°C in both sodium-based and potassium-based buffers and
3) mutual effects of ATP and NO were strongly influenced by particular buffer ionic compositions. Moreover, the presence of potassium facilitated a partial unfolding of alpha-helical structures even at room temperature.
Conclusion
The obtained data might shed more light on molecular mechanisms and biophysics involved in the regulation of protein activity by small solutes in the cell.