Surface magnetism magnetic circular dichroism

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]

A whole range of different properties can be obtained by choosing other interaction operators W t) and thus other V and A operators. Examples are given by Olsen and Jorgensen (1985) and include a diversity of properties such as derivatives of the dipole polarizability, the B term in magnetic circular dichroism, the first anharmonicity of a potential energy surface, two-photon absorption cross sections and derivatives of the dynamic hyperpolarizability. [Pg.210]

The conformations of EAA or acetylacetone (acac) in the complex were studied by means of circular dichroism and magnetic rotatory dispersion spectra (Faraday effect) of the complexes prepared from modeling the species formed on the surface of the catalysts There was good agreement... [Pg.128]

The stmctural and conformational analysis of proteins adsorbed to solid surfaces is difficult because most common analytical methods are not compatible with the presence of the interacting solids. With recent developments in instrumentation and techniques, our understanding of protein adsorption behavior has improved considerably [4, 14]. The most commonly used techniques include attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR), radiolabeling techniques, immunofluorescence enzyme-linked immunosorbent assay (ELISA), ellipsometry, circular dichroism (CD) spectroscopy, surface plasmon resonance (SPR), and amide HX with nuclear magnetic resonance (NMR). Atomic force microscopy (AFM) and scanning... [Pg.266]

The two circular-polarized beams of the incident radiation (I, levorotatory r, dextrorotatory) not only can be influenced with respect to their direction of rotation, but also, in the region of an absorption band, can be absorbed to a different extent by the sample, so that in addition to so-called optical rotatory dispersion (ORD), circular dichroism (CD) or the Cotton effect is observed [35] - (38J. Along with these classical methods of analysis, modem methods for the analytical investigation of surfaces and boundary layers have become very important, including the use of polarized light in ellipsometry ( Surface Analysis) and surface plasmon resonance. Under the influence of external forces (e.g., a magnetic field), even optically inactive substances can be caused to produce magnetooptic rotation. [Pg.428]