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Time-resolved circular dichroism

Xie X and Simon J D 1989 Picosecond time-resolved circular dichroism spectroscopy experimental details and applications Rev. Sol. Instrum. 60 2614-27... [Pg.2970]

Xie X, Simon JD (1990) Picosecond time-resolved circular-dichroism study of protein relaxation in myoglobin following photodissociation of CO. J Am Chem Soc 112 7802-7803... [Pg.235]

The UV/vis spectroscopy [53, 62] and time-resolved Circular Dichroism (TRCD) [63] studies discovered lumi-R and meta-Ra states as the intermediate states between the Pr and Pfr forms. The experimental absorption peak maxima of lumi-R (1.80 eV) and meta-Ra (1.87 eV) states are very close to that of Pr form (1.86eV) [62]. The Cl5=Cl6 rotation is so far accepted as the primary step of the photo-isomerization... [Pg.103]

More esoteric experimental procedures which can be applied to complex molecules include, for example, picosecond time-resolved circular dichroism. A spectrometer for this purpose has been described and used to observe carbon monoxide elimination from excited carbon raonoxymyoglobulin.Fluorescence detected CD has also been used to observe riboflavin in capillary electrophoresis. [Pg.9]

Elove, G.A., Chaffotte, A.F, Roder, H., Goldberg, M.E. Early steps in cytochrome-c folding probed by time-resolved circular-dichroism and fluorescence spectroscopy. Biochemistry 1992,31,6876-83. [Pg.29]

Fig. 16.6 Thee time-resolved circular dichroism (TRCD) of hemoglobin-CO (HbCO dashed line), hemoglobin (Hb solid line) and HbCO 10 is after laser flash photolysis (dotted line). Fig. 16.6 Thee time-resolved circular dichroism (TRCD) of hemoglobin-CO (HbCO dashed line), hemoglobin (Hb solid line) and HbCO 10 is after laser flash photolysis (dotted line).
Early Steps in Cytochrome-c Folding Probed by Time-Resolved Circular-Dichroism and Fluorescence Spectroscopy. [Pg.419]

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]

Bonmarin M, Helbing J (2008) A picosecond time-resolved vibrational circular dichroism spectrometer. Optics Lett 33 2086-2088... [Pg.235]

Circular dichroism (CD), the differential absorption of left versus right cireularly polarized light, is the polarization spectroseopy perhaps best suited to detecting the presence of asymmetry in the structure or environment of moleeular ehromophores. Various time-resolved CD (TRCD) methods have been developed to take advantage of this sensitivity and obtain more detailed structural information about kinetic processes than is found from ordinary time-resolved absorption measurements [33]. Some examples of the processes studied with TRCD methods are the effeets of electronie excitation on the structure of chiral inorganic complexes, the ehanges in a-helical secondary... [Pg.2963]

Sopkova, J., Gallay, J., Vincent, M., Pancoska, P. and Lewit-Bentley, A. 1994. The dynamic behavior of annexin V as a function of calcium ion binding a circular dichroism, UV absorption, and steady-state and time-resolved fluorescence study. Biochemistry. 33, 4490-4499. [Pg.404]

For these purposes, various functional TLMs have already been realized. For exanple, sensitive chiral recognition by circular-dichroism TLM (CD-TLM) was reported for synthesis and analysis of drugs on microchips [6], Other reports have described an electrochemical TLM [7], flow sensing TLM, UV TLM [8], and TLM spectrometer [9]. As important functions for science and technology in micro- and nano-fluidics, three functions are highly desired individual molecule detection as the ultimate sensitivity, fast (real-time) imaging, and femtosecond time-resolved measurement for investigating molecular dynamics in a nano-space. [Pg.2024]

Abstract In the first part of this chapter we will illustrate circular dichroism and we will discuss the optical activity of chemical compounds with respect to light absorption which is at the basis of this technique. Moreover, we will introduce the phenomena that lie behind the technique of optical rotatory dispersion. We thought appropriate to include a brief description of linear dichroism spectroscopy, although this technique has nothing to do with optical activity. In the final part of the chapter we will introduce the basic principles of the luminescence teehniques based on polarized (either circularly or linearly) excitation. The experimental approach to the determination of steady-state and time resolved fluorescence anisotropy will be illustrated. For all the teehniques examined in this chapter the required instrumentation will be schematieally deseribed. A few examples of application of these techniques to molecular and supramolecular systems will also be presented. [Pg.131]


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Time-resolved circular dichroism TRCD)

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