Deconvoluted spectrum

Figure 11 DRIFT spectra of Cu-ZSM-5 at 450 K in 5 kPa CO in Ar. Dashed line is a Fourier self-deconvolution spectrum.

The Wheland intermediate in equation (87) is identified by time-resolved spectroscopy as follows.247 Laser excitation of the EDA complex of NO+ with hexamethylbenzene in dichloromethane immediately generates two transient species as shown in the deconvoluted spectrum in Fig. 20. The absorption band at lmax = 495 nm is readily assigned to the cation radical of... 

Fig. 1.10 (A) Positive mode electrospray spectrum of human gamma interferon on a quadrupole mass analyzer. (B) Deconvoluted spectrum of human gamma interferon. The molecular mass was measured at 16908 2 Da.

Dead time, 7 Dead volume, 13 DEAE cellulose, 88 Deconvolution (spectrum), 215 Deflection equation, 297 Degrees of freedom, 168 Derivative spectrometry 215 Deshielding, 139 Deuterium arc lamp, 199 Diffuse peak, 324 Diffuse reflection, 180 Diffusion coefficient, 5, 102 Diffusion current, 362 Diode array, 200 Distribution isotherm, 9 Double beam, 169 DTGS, 175... 

Values obtained from deconvoluted spectrum. Extinction coefficient in cm-1M 1. s Sample was washed with MeOH to remove magnesium salts. 

A summary of the measured data from the deconvoluted spectrum in Fig. 33 is presented in Table 6. Based on these data the polydispersity is calculated to be 1.0007, which is a significant step toward producing a monodisperse macro-molecular system. 

In order to assess the size of the carbohydrate component, deglycosylated CHO IL-4 by A-glycanase was analyzed by ESI-MS. The deconvoluted spectrum displayed an MW of 14,955 Da, which conformed well to the theoretical MW of the protein (MW 14,963 Da) when considering the presence of three disulfide bonds in the protein. 

Figure 19-12. Positive-ion ESI mass spectrum of CHO IL-4. (A) Raw spectrum and (B) deconvoluted spectrum. (Reprinted from reference 69, with permission of John Wiley Sons, Ltd.)...

Since incubation of the protease with a large excess of DFP could nonspecifically phosphorylate tyrosine residues (10), the control and inactivated protease samples were analyzed by ES mass spectrometry (8). The ES mass spectrum of a fully active control sample of CMV protease is shown in Figure 1, where a series of multiply charged ions (from +12 to +34) provided an average Mf value of 27,910 (calculated Mr=27,909). The deconvoluted spectrum (Fig. 1, inset), shows that only 30% of the protease was full length (observed... 

Mr=28,040). The remaining 70% corresponds to the protease lacking the amino terminal methionine residue (desMet-protease Mr=27,910). Figure 2 compares the deconvoluted spectrum of a control protease sample (Panel A) with that of a protease sample (180 xM) which had been completely inactivated by a 3-hour incubation with 4 mM DFP (Panel B). As expected, no unsubstituted protease was detectable in the spectrum in Panel B. 

Figure 1. A, SDS-PAGE analysis. From the left- standard (45, 31, 21 and 14 kDa, from the top), DTT-reduced rhSCF, DTT-reduced dimer, nonreduced rhSCF, and nonreduced dimer. B, RP-HPLC of wild type rhSCF and the SDS-nondissociable dimer. C. ESI-MS analysis of wild type rhSCF and the dimer. The multiply charged ions are indicated and the molecular masses of each form obtained from the respective deconvoluted spectrum are 18,658.5 2.3 and 37,315.2+3.6, respectively.

FIGURE 3.10 Deconvoluted spectrum of the 50 x dilution of the extract. Based on base composition calculations, the corresponding sequence for the three cleavage products are shown, r.i. = relative intensity. 

Figure 5.5 RPLC-MS of pi fractions. A-G represent pi ranges of 9.2-8.1, 8.1-7.0, 7.0 5.9, 5.9-4.8, 4.8-3.7, 3.7-2.6 and 2.6-1.5, respectively. Left panel, extracted mass chromatogram of each protein in the fraction middle panel, raw spectrum of each protein averaged over the top 80% of the LC peak right panel, deconvoluted spectrum (singly charged) by MaxEntl. Only the total ion chromatogram is shown for fraction F no deconvoluted spectrum is shown for fraction G. Reprinted with permission from F. Zhou and M. Johnston, Analytical Chemistry 76, 2734—2740, Copyright 2004 American Chemical Society...

The raw and deconvoluted mass spectra from scans 2000-2025 of the eighth protein fraction are shown in Figure 5.9a and b, as an example of proteins that are not isotopicafly resolved. The most intense feature of the deconvoluted spectrum in Figure 5.9b, 16293 Da,... 

Figure 3. 29Si NMR spectra of Compol. Part a Direct polarization MAS, 300 accumulations, and repetition time of 400 s. Part b Deconvoluted spectrum using Gaussian line shape. Continued on next page.

Fig. 10. Mass spectra of from MALDIMS, and from ESIMS. For MALDIMS the mass scale was calibrated with myoglobin ions as an internal standard. For ESIMS the mass scale was calibrated externally using the doubly charged and singly charged ions of gramicidin S. The right hand panel of the ESIMS spectrum shows the deconvoluted spectrum, giving measured molecular weights for the mtgor species, which differ by one hexose. Deviations from the calculated values are shown in parentheses.

Similarly the concentrations of individual components in the exit stream as analyzed by mass spectrometry may or may not be correctly represented by the intensity of the parent peak of the said component. Two steps are required to transform the raw data to kinetically useful quantities. The first step stems from the fact that each mass peak may contain contributions from a number of components in the effluent. To resolve this difficulty, a mathematical procedure called deconvolution is applied to the observed total mass spectrum of the exit stream from the reactor. Deconvolution allows us to separate the total intensities at individual mass numbers into their several components, each of which is due to a contribution arising from the spectrum of an individual constituent present in the effluent sample. The deconvoluted spectrum then reports the mol fractions of the individual components in the effluent. With this in hand, the next step is to transform the output mol fractions to concentrations so they can be used in rate expressions to correlate reaction rates. 

Fig. 4.18. The deconvoluted spectrum of lactose permease showing a molecular weight of 47,357 Da (redrawn with permission from J.P. Whitelegge et al. PNAS, 1999, 96 10695-10698, copyright 1999, National Academy of Sciences, U.S.A.).

Fig. 5.12 The mass spectrum of myoglobin showing multiply charged ions (upper trace) and the deconvoluted spectrum showing the molecular weight (lower trace).

Figure 5 (Left) GCxGC-ToF MS contour plot for m/z 197 for a tobacco extract containing chlorpyrifos (black circle) using an Rtx-lxRtx-200 column set. (Right) Caliper spectrum unresolved spectrum at the peak apex where chlorpyrifos elutes. Peak true deconvoluted spectrum. Reference spectrum of chlorpyrifos standard [14].

FIGURE 8.3 Si NMR spectra of Compol. (a) Direct polarization MAS, 300 accumulations, and repetition time of 400 s. (b) Deconvoluated spectmm using Gaussian line shape. 2 Si NMR spectra of Compol. (c) CP-MAS, 2000 accumulations, repetition time of 4 s, and contact time of 4 ms. (d) Deconvoluted spectrum using Gaussian line shape. 

High-resolution Si MAS NMR of silicalite (B) compared with that from a ZSM-5 (containing aluminium but with the same framework structure). (C) shows the deconvoluted spectrum for comparison, and indicates the 24 different resonances. [Reproduced from reference 99 with permission. Copyright 1988 American Chemical Society.]... 

Fourier analysis offers the process of selfdeconvolution that is capable of resolving imder-lying peaks from broad overlapping bands. Fourier self-deconvolution has the advantage over derivati-zed spectra that there is no shift or averaging effect and the self-deconvoluted spectrum is directly comparable with the log/reciprocal wavelength scale. 

Fig. 28. Spectra and proposed structure of films absorbed onto substrate. (Top) Spectra in the mid-frequency region of n-Ci5H3iC02H as a film adsorbed on AI2O3 (top) and in a KBr matrix (bottom). The KBr experimental spectrum is accompanied by a deconvoluted spectrum (dashed curve), which represents enhanced resolution. n-Ci5H3iC02H (Bottom) Proposed structure of the adsorbed species having fully extended chains. The molecular orientation is defined relative to the surface coordinates (206).

---