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Fourier-transform infrared continued

Spectroscopy. Infrared spectroscopy (48) permits stmctural definition, eg, it resolves the 2,2 - from the 2,4 -methylene units in novolak resins. However, the broad bands and severely overlapping peaks present problems. For uncured resins, nmr rather than ir spectroscopy has become the technique of choice for microstmctural information. However, Fourier transform infrared (ftir) gives useful information on curing phenoHcs (49). Nevertheless, ir spectroscopy continues to be used as one of the detectors in the analysis of phenoHcs by gpc. [Pg.299]

Fourier transform infrared (FTIR) analyzers can be used for industrial applications and m situ measurements in addition to conventional laboratory use. Industrial instruments are transportable, rugged and relatively simple to calibrate and operate. They are capable of analyzing many gas components and determining their concentrations, practically continuously. FTIR analyzers are based on the spectra characterization of infrared light absorbed by transitions in vibrational and rotational energy levels of heteroatomic molecules. [Pg.1303]

Figure 23-3 Infrared absorbance spectra of the amide regions of proteins. (A) Spectra of insulin fibrils illustrating dichroism. Solid line, electric vector parallel to fibril axis broken line, electric vector perpendicular to fibril axis. From Burke and Rougvie.24 Courtesy of Malcolm Rougvie. See also Box 29-E. (B) Fourier transform infrared (FTIR) spectra of two soluble proteins in aqueous solution obtained after subtraction of the background H20 absorption. The spectrum of myoglobin, a predominantly a-helical protein, is shown as a continuous line. That of concanavalin A, a predominantly (3-sheet containing protein, is shown as a broken line. From Haris and Chapman.14 Courtesy of Dennis Chapman. Figure 23-3 Infrared absorbance spectra of the amide regions of proteins. (A) Spectra of insulin fibrils illustrating dichroism. Solid line, electric vector parallel to fibril axis broken line, electric vector perpendicular to fibril axis. From Burke and Rougvie.24 Courtesy of Malcolm Rougvie. See also Box 29-E. (B) Fourier transform infrared (FTIR) spectra of two soluble proteins in aqueous solution obtained after subtraction of the background H20 absorption. The spectrum of myoglobin, a predominantly a-helical protein, is shown as a continuous line. That of concanavalin A, a predominantly (3-sheet containing protein, is shown as a broken line. From Haris and Chapman.14 Courtesy of Dennis Chapman.
Kakuta, M., Hinsman, P., Manz, A., Lendl, B., Time-resolved Fourier transform infrared spectrometry using a microfabricated continuous flow mixer application to protein conformation study using the example of ubiquitin, Lab Chip 2003, 3, 82-85. [Pg.277]

There continues to be major problems with coupling HPLC to FTIR (Fourier transform infrared) due to the interference caused by water. The interface is the critical component in the system [126]. The two basic types of interfaces are continuous and capture. A continuous interface has been developed that uses a liquid-liquid extraction. In this approach, the analytes are extracted from the mobile phase by mixing postcolumn with a stream of IR (infrared) transparent, water-immiscible solvent. In the ca-pure technique, the eluent is deposited on a continuously moving, IR transparent, inert substrate from which the eluent can be easily removed by evaporation. These techniques have been applied to identification of racemic precursors of diltizam, AZT derivatives, and steroids [127]. [Pg.79]

Apparatus Use a Fourier transform infrared spectrometer (FTIR), with its associated computer and peripherals, capable of measuring from 4500 to 500 cm-1 and of acquiring data with a resolution of at least 2 cm-1. The optics of the instmment must be sealed and desiccated, or, like the sample chamber, must be under continuous dry air or nitrogen gas purge. The spectrometer is equipped with software capable of multicomponent analysis using the partial least squares method (PLS-1, or equivalent). This software is commercially available as an accessory to the spectrometer or as an external software package. [Pg.895]

Vibrational spectroscopy is an important tool for the characterization of various chemical species. Valuable information regarding molecular structures as well as intra- and intermolecular forces can be extracted from vibrational spectral data. Recent advances, such as the introduction of laser sources to Raman spectroscopy, the commercial availability of Fourier transform infrared spectrometers, and the continuing development and application of the matrix-isolation technique to a variety of chemical systems, have greatly enhanced the utility of vibrational spectroscopy to chemists. [Pg.231]

IR spectra were taken at room temperature (300 K) and liquid-helium temperatures (5-15 K), using a Bomem DAS Fourier transform infrared (FTIR) spectrometer and an InSb detector. For the low-temperature measurements, a Janis continuous-flow liquid-helium cryostat with wedged, IR-transparent windows was utilized. Hall-effect measurements, in the Van der Pauw geometry, were performed at room temperature using a system from MMR Technologies. Wires were attached to the ZnO using silver paint, which provided adequate Ohmic contacts for the electron concentrations (10 cm ) in these samples. [Pg.126]

Fourier Transform Infrared Spectroscopy Table 4.1.2. (continued)... [Pg.365]

Fourier-transform infrared spectroscopy (FTIR) and pH measurements are the techniques most often adapted for in-line IPC. pH measurements are used for reactions that are run in water or have an aqueous component, e.g., an aqueous extraction. FTIR is especially good for monitoring continuous reactions [12] and reactions that would be dramatically changed by exposure to the atmosphere and temperature of the laboratory. Suitable reactions include low-temperature reactions, reactions run under pressure, reactions with gaseous or toxic materials (e.g., ethylene oxide), and reactions run under inert atmosphere. Further advantages of in-line assays are that no samples need to be prepared, and assay results can be generated within minutes. [Pg.159]

Fourier transform infrared spectrophotometry is used widely in the semiconductor industry for the routine determination of the interstitial oxygen content of production silicon wafers. However, the lack of interlaboratory reproducibility in this method has forced the use of ad-hoc calibration methods. The sources of this lack of reproducibility are just beginning to be understood. As investigation of this problem continues and wider acceptance is gained for improved experimental and analytical techniques, a greater degree of reproducibility should be achieved. Furthermore, new standard test methods and standard reference materials being developed by the ASTM (71 ),... [Pg.226]

Fig. 1.1 Archaeological science in the field. Excavations in the background supply samples for a Fourier Transform Infrared Spectrometer, center, and microscopic identification, foreground. This project is at Tell es-Safi/Gath, an archaeological site in Israel occupied almost continuously from prehistoric to modem times. Photo courtesy of Kimmel Center for Archaeological Science, Weizmann Institute of Science, Israel... Fig. 1.1 Archaeological science in the field. Excavations in the background supply samples for a Fourier Transform Infrared Spectrometer, center, and microscopic identification, foreground. This project is at Tell es-Safi/Gath, an archaeological site in Israel occupied almost continuously from prehistoric to modem times. Photo courtesy of Kimmel Center for Archaeological Science, Weizmann Institute of Science, Israel...

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Continuous Fourier transformation

Fourier transform infrared

Infrared (continued

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