Corrective ramp

For calculating effective mobilities for identification purpose, voltage ramping needs to be corrected. ... 

Figure 5. Arrhenius plot for mixed system to B-stage cure uncorrected vs. corrected plots for curing of the neat resin during temperature ramping.

Manipulated inputs, u Variables such as pressure, time of pressure application, first and second hold temperatures, first and second temperature hold durations, and temperature ramp rates. These variables represent changes in regulatory controller set points with time, the time sequence of process events, and corrective actions that can be taken during the process. 

At higher temperatures a significant amount of reaction may occur during the initial temperature ramp before approximate isothermal equilibrium has been attained. Some degree of correction for this is possible 16,17) by re-running the experiment on the reacted sample, under the same conditions, to obtain an estimate of the true baseline, as illustrated in Fig. 4. 

Shaped pulses are created from text files that have a line-by-line description of the amplitude and phase of each of the component rectangular pulses. These files are created by software that calculates from a mathematical shape and a frequency shift (to create the phase ramp). There are hundreds of shapes available, with names like Wurst , Sneeze , Iburp , and so on, specialized for all sorts of applications (inversion, excitation, broadband, selective, decoupling, peak suppression, band selective, etc.). The software sets the maximum RF power level of the shape at the top of the curve, so that the area under the curve will correspond to the approximately correct pulse rotation desired (90°, 180°, etc.). When an experiment is started, this list is loaded into the memory of the waveform generator (Varian) or amplitude setting unit (Bruker), and when a shaped pulse is called for in the pulse sequence, the amplitudes and phases are set in real time as the individual rectangular pulses are executed. 

Figure 19. Resonance Raman spectra of the oxidized Mo domain of recombinant human SO. (a) The Mo domain prepared by tryptic cleavage of the K108R variant of the holoenzyme. (b) His-tagged Mo-domain. Spectra recorded using 488-nm excitation for samples (0.5-1.0 mM in Mo) in 50-mM tricine buffer, pH 8.0, frozen at 17-25 K. Bands marked an asterisk correspond to lattice modes of ice and bands marked with P correspond to nonresonantly enhanced protein modes. A linear ramp has been subtracted to correct for a sloping fluorescence background.

DMSOR obtained with 568-nm excitation and (b) of thionine-oxidized P. furiosus FOR obtained with 530-nm excitation. The spectra were recorded using samples ( 3 mM) frozen at 25 K. The buffering medium was a 50 mM Tris buffer, pH 7.8 for FOR and 50 mM tricine, pH 7.5 for DMSOR. Bands marked s correspond to residual DMSO and bands marked with p correspond to nonresonantly enhanced protein modes. A linear ramp has been subtracted to correct for a sloping fluorescence background. 

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