Spectroscopy Fourier transform resonance Raman

Matysik J, Hildebrand P, Schlamann W, Braslavsky SE, Schaffner K (1995) Fourier-transform resonance Raman spectroscopy of intermediates of the phytochrome photocycle. [Pg.191]

Mattioli, T.A., Hoffman, A., Robert, B., Schrader, B., Lutz, M. Primary donor structure and interactions in bacterial reaction centCTs from near-infrared Fourier-transform resonance Raman spectroscopy. Biochemistry 30, 4648-4654 (1991)... [Pg.544]

Recently we improved the reaction center isolation procedure - A purified preparation still containing the H subunit, and displaying a stable photochemical activity, was obtained - In this article we will compare some functional properties of this reaction center preparation with reference to Rhodopseudomonas viridis and Rhodobacter sphaeroides. Similarities are found with the former at the level of the acceptor quinone complex the structure of the primary donor in both the reduced and oxidized states, as determined by Fourier transform resonance Raman spectroscopy, resembles the latter. [Pg.133]

Infrared and nuclear magnetic resonance spectroscopy are the most important spectroscopic methods for analyzing coating materials. Near infrared Fourier transform (NIRFT) Raman spectroscopy [10.8] also has great potential, particularly for aqueous systems. UV/VIS spectroscopy is used only in exceptional cases, e.g., to determine light protection agents (UV absorbers). [Pg.236]

With recent developments in analytical instrumentation these criteria are being increasingly fulfilled by physicochemical spectroscopic approaches, often referred to as whole-organism fingerprinting methods.910 Such methods involve the concurrent measurement of large numbers of spectral characters that together reflect the overall cell composition. Examples of the most popular methods used in the 20th century include pyrolysis mass spectrometry (PyMS),11,12 Fourier transform-infrared spectrometry (FT-IR), and UV resonance Raman spectroscopy.16,17 The PyMS technique... [Pg.322]

Probing Metalloproteins Electronic absorption spectroscopy of copper proteins, 226, 1 electronic absorption spectroscopy of nonheme iron proteins, 226, 33 cobalt as probe and label of proteins, 226, 52 biochemical and spectroscopic probes of mercury(ii) coordination environments in proteins, 226, 71 low-temperature optical spectroscopy metalloprotein structure and dynamics, 226, 97 nanosecond transient absorption spectroscopy, 226, 119 nanosecond time-resolved absorption and polarization dichroism spectroscopies, 226, 147 real-time spectroscopic techniques for probing conformational dynamics of heme proteins, 226, 177 variable-temperature magnetic circular dichroism, 226, 199 linear dichroism, 226, 232 infrared spectroscopy, 226, 259 Fourier transform infrared spectroscopy, 226, 289 infrared circular dichroism, 226, 306 Raman and resonance Raman spectroscopy, 226, 319 protein structure from ultraviolet resonance Raman spectroscopy, 226, 374 single-crystal micro-Raman spectroscopy, 226, 397 nanosecond time-resolved resonance Raman spectroscopy, 226, 409 techniques for obtaining resonance Raman spectra of metalloproteins, 226, 431 Raman optical activity, 226, 470 surface-enhanced resonance Raman scattering, 226, 482 luminescence... [Pg.457]

This expression for the complete overlap is Fourier transformed to give the electronic emission spectrum. In order to carry out the calculation it is necessary to know the frequencies and the displacements for all of the displaced normal modes. In addition, the energy difference between the minima of the two potential surfaces E0 and the damping r must be known. As will be discussed below, the frequencies and displacements can be experimentally determined from pre-resonance Raman spectroscopy, and the energy difference between the ground and excited states and the damping can be obtained from the electronic absorption spectrum and/or emission spectrum. [Pg.43]

Developments in Raman spectroscopy, with applications for colorants, have included resonance Raman, surface enhanced Raman spectroscopy (SERS), surface enhanced resonance Raman spectroscopy (SERRS) and near-infrared Fourier transform Raman spectroscopy (NIR-FT-Raman), with the latter technique discussed in the next section. [Pg.295]

Fourier transform techniques in spectroscopy [5-7] that are useful in chemistry include all kinds of spectroscopy, in particular, infrared spectroscopy [8] and Raman spectroscopy [9], mass spectrometry, nuclear magnetic resonance spectroscopy [10], and X-ray crystallography [11],... [Pg.435]

Characterization of Lignin. Lignin is characterized in the solid state by Fourier transform infrared (ftir) spectroscopy, uv microscopy, interference microscopy, cross polarization/magic angle spinning nuclear magnetic resonance (cp/mas nmr) spectroscopy, photoacoustic spectroscopy, Raman spectroscopy. [Pg.4241]

Raman spectroscopy is a vibrational spectroscopic technique which can be a useful probe of protein structure, since both intensity and frequency of vibrational motions of the amino acid side chains or polypeptide backbone are sensitive to chemical changes and the microenvironment around the functional groups. Thus, it can monitor changes related to tertiary structure as well as secondary structure of proteins. An important advantage of this technique is its versatility in application to samples which may be in solution or solid, clear or turbid, in aqueous or organic solvent. Since the concentration of proteins typically found in food systems is high, the classical dispersive method based on visible laser Raman spectroscopy, as well as the newer technique known as Fourier-transform Raman spectroscopy which utilizes near-infrared excitation, are more suitable to study food proteins (Li-Chan et aL, 1994). In contrast the technique based on ultraviolet excitation, known as resonance Raman spectroscopy, is more commonly used to study dilute protein solutions. [Pg.15]

Merlin, J.C., Comard, J.P., Statoua, A., Saidi-Idrissi, M., Lautie, M.F. Brouillard, R. (1994). Vibrational analysis of hydrox3dlavylium derivatives by IR, Fourier transform Raman and resonance Raman spectroscopies. SpectrochimicaActa, 50, 703-712. [Pg.21]

UV-visible absorption/reflection Electron spin resonance Raman spectroscopy Fourier transform infrared spectroscopy Probe beam deflection Scanning tunneling microscopy Scanning electrochemical microscopy Work function measurements In situ electrical conductivity 144, 277, 373-382 247, 369. 375,. 383, 384 144, 385-389 390, 391 156, 392, 393. 394, 395 3%, 397 172, 173 256, 289, 290, 398-401... [Pg.570]

Fourier transform Raman and resonance Raman spectroscopies. Spectrochim. [Pg.283]

Silicone elastomers are covalently crosslinked networks with an effective infinite molecular weight and are, as such, insoluble and intractable. Consequently the interrogative spectroscopic and imaging methodologies that may be employed to probe such a network structure are almost wholly confined to the solid state. Surface vibrational spectroscopies attenuation total reflectance Fourier transform infrared (ATR-FTIR) and resonance Raman spectroscopy... [Pg.153]

The crystalline mineral silicates have been well characterized and their diversity of stmcture thoroughly presented (2). The stmctures of siHcate glasses and solutions can be investigated through potentiometric and dye adsorption studies, chemical derivatization and gas chromatography, and laser Raman, infrared (ftir), and Si Fourier transform nuclear magnetic resonance ( Si ft-nmr) spectroscopy. References 3—6 contain reviews of the general chemical and physical properties of siHcate materials. [Pg.3]