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Spectrometers recording

A laser pulse strikes the surface of a specimen (a), removing material from the first layer, A. The mass spectrometer records the formation of A+ ions (b). As the laser pulses ablate more material, eventually layer B is reached, at which stage A ions begin to decrease in abundance and ions appear instead. The process is repeated when the B/C boundary is reached so that B+ ions disappear from the spectrum and C+ ions appear instead. This method is useful for depth profiling through a specimen, very little of which is needed. In (c), less power is used and the laser beam is directed at different spots across a specimen. Where there is no surface contamination, only B ions appear, but, where there is surface impurity, ions A from the impurity also appear in the spectrum (d). [Pg.11]

Both Porter s original flash photolysis apparatus and Pimentel s rapid scan spectrometer recorded the whole spectral region in a time which was short compared to the decay of the transient species. Kinetic information was obtained by repeatedly firing the photolytic flash lamp and making each spectroscopic measurement at a different time delay after each flash. The decay rate could then be extracted from this series of delayed spectra. Such a process clearly has limitations, particularly for IR measurements, where the decay must be slow compared to the scan rate of the spectrum. [Pg.289]

L22 (a) Sketch the first derivative of a Lorentz line shape, (b) Some ESR spectrometers record the second derivative (rather than the first derivative) of resonance lines. Sketch the second derivative of a Lorentzian line, indicating the position of Pq. [Pg.446]

Fig. 3. Experimental arrangement for observing oriented fibre spectra in the Cary 81 spectrometer. Recording positions are shown by a), b), and c). b) and c) are equivalent due to the cylindrical symmetry of the sample about the fibre axis... Fig. 3. Experimental arrangement for observing oriented fibre spectra in the Cary 81 spectrometer. Recording positions are shown by a), b), and c). b) and c) are equivalent due to the cylindrical symmetry of the sample about the fibre axis...
The peaks of the mass spectrum often differ by a factor of several hundred in their intensity. Therefore, the registering system of a mass spectrometer records the spectrum simultaneously by several channels which differ in the magnitude of amplification. [Pg.43]

Johann-type crystal spectrometers record an energy interval according to the size of the source simultaneously, if a position-sensitive X-ray detector of corresponding extension is available. The use of spherically-bent crystals allows partial vertical focusing, which increases the count rate by a factor of almost two for Bragg angles around 55°. [Pg.502]

A 300-MHz spectrometer records a proton that absorbs at a frequency 2130 Hz downfield (deshielded) from TMS. [Pg.569]

Infrared and Raman spectrometers usually combine a radiation source, a sample arrangement, a device for spectral dispersion or selection of radiation, and a radiation detector, connected to appropriate recording and evaluation facilities. An ideal spectrometer records completely resolved spectra with a maximum signal-to-noise ratio. It requires a minimum amount of sample which is measured nondestructively in a minimum time, and it provides facilities for storing and evaluating the spectra. It also supplies information concerning composition, constitution, and other physical properties. In practice, spectrometers do not entirely meet all of these conditions. Depending on the application, a compromise has to be found. [Pg.63]

The mass spectrometer records a spectrum of the individual components. [Pg.469]

Unlike ultraviolet and nmr spectra, infrared spectra are inverted and are not always presented on the same scale. Some spectrometers record the spectra on an ordinate linear in microns, but this compresses the low wavelength region. Other spectrometers present the spectra on a scale linear in reciprocal centimeters, but linear on two different scales, one between 4000 and 2000 cm , which spreads out the low wavelength region, and the other, a smaller scale Ijetween 200 and 667 cm . ... [Pg.203]

For a complicated spectrum, it may be helpful to operate on a reduced-size data set. Many spectrometers record absorbance readings at 1-nm intervals a complete UV-visible spectrum (200-700 nm) contains 500 data points. If the spectrum contains eight bands, you re performing calculations on more than 4000 cells. Start with a data set consisting of every 10th data point, for example. After you have achieved a reasonably good fit to this data set, use these values as initial parameters for the complete data set. [Pg.347]

A laser pulse strikes the surface of a specimen (a), removing material from the first layer, A. The mass spectrometer records the formation of A ions (b). As the laser pulses ablate more material, eventually layer B is reached, at which stage A ions begin to decrease in abundance and B ions appear instead. Tlie process is repeated when tlie B/C boundary is reached so ... [Pg.15]

The mass spectrometer records a mass spectrum—a graph of the relative abundance of each fragment plotted against its m/z value. Because the charge (z) on essentially all the fragments that reach the collector plate is -1-1, m/z is the molecular mass (m) of the fragment. Remember that only positively charged species reach the collector. [Pg.485]

Mass spectrometry allows us to determine the molecular mass and the molecular formula of a compound, as well as certain structural features. In mass spectrometry, a small sample of the compound is vaporized and then ionized as a result of an electron s being removed from each molecule, producing a molecular ion—a radical cation. Many of the molecular ions break apart into cations, radicals, neutral molecules, and other radical cations. The bonds most likely to break are the weakest ones and those that result in the formation of the most stable products. The mass spectrometer records a mass spectrum—a graph of the relative abundance of each positively charged fragment, plotted against its mjz value. [Pg.516]

The spectrum records the amount of radiation transmitted at each frequency, so the maximum absorption occurs when the least light is transmitted, and the recorder line is closest to the bottom of the spectrum. Positions of maximum absorption are difficult to measure accurately from the spectrum, so most spectrometers record them automatically, and print them alongside the spectrum, giving the % of radiation transmitted (%7) alongside. The machine can be set to record frequencies of all or only the stronger peaks. [Pg.2]

Once again, this is very like the situation in a carboxylic acid. The two enols equilibrate (tautomerize) so fast in CDCI3 solution that the NMR spectrometer records an averaged spectrum. By contrast, equilibration between the enol and keto forms is sufficiently slow that the NMR spectrometer records separate signals for the keto and enol forms. [Pg.458]

The Fellgett or multiplex advantage deals with the fact that a Fourier transform spectrometer records data from the entire spectral region throughout the experiment. This is quite different to the case with a dispersive spectrometer, as the grating or prism instrument only measures a narrow bandwidth at any time. The measurement bandwidth of the dispersive spectrometer is regulated by the instrument s exit slit. This difference has important effects on the acquisition of data. [Pg.406]

An NMR spectrometer records resonance as a signal, and the collection of all resonance signals for a sample is its NMR spectrum. [Pg.399]

FIGURE 3.2 Schematic representations of MALDI-IMS procedures. Usually, the tissue section mounted on an indium thin oxide (ITO)-coated glass shde is covered with a specific MALDI matrix. Next, the ITO slide is inserted into a mass spectrometer. The MALDI laser scans through a set of preselected locations on the tissue (10-200 pm scan pitch) and the mass spectrometer records the spatial distribution of molecular species. Suitable image processing software can be used to import data from the mass spectrometer to allow visualization and comparison with the histological image of the sample. [Pg.43]


See other pages where Spectrometers recording is mentioned: [Pg.313]    [Pg.314]    [Pg.427]    [Pg.133]    [Pg.80]    [Pg.408]    [Pg.6]    [Pg.466]    [Pg.47]    [Pg.314]    [Pg.470]    [Pg.1131]    [Pg.15]    [Pg.313]    [Pg.136]    [Pg.253]    [Pg.299]    [Pg.970]    [Pg.314]    [Pg.30]    [Pg.306]    [Pg.321]    [Pg.307]    [Pg.411]    [Pg.504]    [Pg.2524]    [Pg.655]    [Pg.227]    [Pg.41]   
See also in sourсe #XX -- [ Pg.355 ]

See also in sourсe #XX -- [ Pg.355 ]




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Circular dichroism recording spectrometer

Spectrometers double-beam recording

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