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Residual/error spectra

Even though restoration in two distinct spectral bands leads to very fast algorithms, it is still not optimum because of the residual error in the low-frequency band of spectral components used as a region of support. Perhaps the requirement that the inverse-filtered low-frequency spectrum (or, equivalently, its corresponding spatial function) be held constant for the restoration... [Pg.285]

Figure 114 The four elementary hydration spectra Hj(P) (i = 1 ) of HA, together with the residual spectrum with greatest features, labelled greatest error spectrum . Spectra are offset for clarity. Figure 114 The four elementary hydration spectra Hj(P) (i = 1 ) of HA, together with the residual spectrum with greatest features, labelled greatest error spectrum . Spectra are offset for clarity.
Multi-component analysis can be readily apphed to the infrared spectra of minerals. The latter contain non-interacting components and so the spectrum of a mineral can be analysed in terms of a linear combination of the spectra of the individual components. However, the spectra of such solids exhibit a marked particle-size dependency. The particle size should be reduced (to 325 mesh) prior to preparation of an alkali halide disc. The pellet preparation involves separate grinding and dispersion steps because minerals tend not to be effectively ground in the presence of an excess of KBr. Figure 5.8 illustrates the analysis of a mineral containing several components. The sample spectrum (a) is shown, as well as the calculated spectrum (b) based on the reference spectra of a variety of standard mineral components. The residual difference spectrum (c) shows that the error between the two spectra is small. [Pg.107]

Calibration Measurement Residuals Plot (Model Diagnostic) The calibration spectral residuals shown in Figure 5-53 are still structured, but are a factor of 4 smaller than the residuals when temperature was not part of the model Comparing with Figure 5-51, the residuals structure resembles the estimated pure spectrum of temperature. Recall that the calibration spectral residuals are a function of model error as well as errors in the concentration matrix (see Equation 5.18). Either of these errors can cause nonrandom features in the spectral residuals. The temperature measurement is less precise relative to the chemical concentrations and, therefore, the hypothesis is that the structure in the residuals is due to temperature errors rather than an inadequacy in the model. [Pg.301]

One of the main motivations of using synthetic DNA for cellular engineering seems to be at odds with the random nature of directed evolution. Traditionally, PCR-based methods have been used to create sequence diversity, inspired by the fact that mutations in nature commonly arise from errors in DNA replication. PCR-based methods are preferred when there is no prior knowledge about where mutations are likely to influence the traits of interest, but are limited in that the sequence diversity that results is restricted and biased. With single base mutations per codon - a common assumption with most protocols - only 5.7 amino acids are accessible per position on average, and in most cases, the resulting set of amino acids does not accurately represent the spectrum of physicochemical properties of naturally-occurring residues [76]. [Pg.121]

Another possibility to select optimal wavelengths is the variance-covariance matrix [68]. The fundamental problem of this approach is that the algorithm tries to minimise the residual vector. If an additional unknown concentration is hidden in the spectrum measured, interactions between the reactants exist which were not taken into account in the calibration. Therefore the algorithm has to result in an error. This means the solution a has to be erroneous. In this case the minimisation of the least squares sums, the variance, has to give an erroneous result in principle. This means that for some of the concentrations, a wrong amount is added to compensate for the additional compound or the interaction. [Pg.271]

In wt another NMR example, Sykes et a1. used a DISPA analysis of the 1"F NMR spectrum for M13 coat protein the DISPA data points were located on the reference circle, within experimental error, showing that the two fluorotyrosines exhibited the same chemical shift.22 Subsequent experiments based on solvent shifts confirmed that both fluorinated amino acid residues were "buried" and not accessible to solvent. [Pg.118]

Fig. 5. MCR-ALS calculations of the deprotonation of trityl-protected lb (a) calculated absorption profiles, (b) spectra calculations, (c) pure substance lb spectrum. MCR-ALS-Parameters [efa matrix]=efa(depl0,90) min value of log efa plot=l number of factors=2 als2004 Data matrix=deplO Init estimate=efa matrix Non negative Concentration nnls number of spec with non neg=2 spec equal height Plots are optimum in the iteration Nr. 935 Std.dev of residuals vs. exp. data=0.0011238 Fitting error (lack of fit, lof) in % (PCA)=2.8319e-014 Fitting error (lack of fit, lof) in %(exp)=4.881 Percent of variance explained at the optimum is=99.7618. Figure reproduced from Lumpi et al., 2009. Fig. 5. MCR-ALS calculations of the deprotonation of trityl-protected lb (a) calculated absorption profiles, (b) spectra calculations, (c) pure substance lb spectrum. MCR-ALS-Parameters [efa matrix]=efa(depl0,90) min value of log efa plot=l number of factors=2 als2004 Data matrix=deplO Init estimate=efa matrix Non negative Concentration nnls number of spec with non neg=2 spec equal height Plots are optimum in the iteration Nr. 935 Std.dev of residuals vs. exp. data=0.0011238 Fitting error (lack of fit, lof) in % (PCA)=2.8319e-014 Fitting error (lack of fit, lof) in %(exp)=4.881 Percent of variance explained at the optimum is=99.7618. Figure reproduced from Lumpi et al., 2009.

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See also in sourсe #XX -- [ Pg.249 , Pg.250 ]




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Error residual

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