Raman spectroscopy conformation

In this review the definition of orientation and orientation functions or orientation averages will be considered in detail. This will be followed by a comprehensive account of the information which can be obtained by three spectroscopic techniques, infra-red and Raman spectroscopy and broad line nuclear magnetic resonance. The use of polarized fluorescence will not be discussed here, but is the subject of a contemporary review article by the author and J. H. Nobbs 1. The present review will be completed by consideration of the information which has been obtained on the development of molecular orientation in polyethylene terephthalate and poly(tetramethylene terephthalate) where there are also clearly defined changes in the conformation of the molecule. In this paper, particular attention will be given to the characterization of biaxially oriented films. Previous reviews of this subject have been given by the author and his colleagues, but have been concerned with discussion of results for uniaxially oriented systems only2,3). 

Ultraviolet/visible absorption, fluorescence, infrared and Raman spectroscopies are useful for studying structures (configuration, conformation, symmetry etc.) of electronically ground and excited states of linear polyenes, which have attracted much attention of... 

Measurements of the proximal histidine-iron stretching frequency by Resonance Raman spectroscopy revealed that this bond is very weak in relation to other heme protein systems (vFe.His = 204 cm-1) (130). Formation of the sGC-NO complex labilizes this ligand resulting in the formation of a 5-coordinate high spin iron(II) complex, and the conformational change responsible for the several hundred-fold increase in catalytic activity (126,129,130). 

Recent studies on PEO-PPO, PEO-PBO di- and triblock copolymers include the works of Bahadur et al. [121], who examined the role of various additives on the micellization behavior, of Guo et al. [122], who used FT-Raman spectroscopy to study the hydration and conformation as a function of temperature, of Booth and coworkers [ 123], who were mainly interested in PEO-PBO block copolymers with long PEO sequences, and of Hamley et al., who used in situ AFM measurements in water to characterize the morphology of PEO-PPO micelles [56,57]. 

Information concerning conformation, tacticity and crystallinity may also be obtained (1). Vibrational transitions accesssible to IR spectroscopy are governed by the selection rule that there must be a change in dipole moment during excitation of the polymer vibrations. Thus symmetric vibrations which are detected by Raman spectroscopy are inaccessible to IR absorption measurements. 

Further details of the theory and application of Raman spectroscopy in polymer studies can be found elsewhere (1. 9). However, vibrational frequencies of functional groups in polymers can be characterized from the spacing of the Raman lines and thus information complementary to IR absorption spectroscopy can be obtained. In addition, since visible radiation is used the technique can be applied to aqueous media in contrast to IR spectroscopy, allowing studies of synthetic polyelectrolytes and biopolymers to be undertaken. Conformation and crystallinity of polymers have also been shown to influence the Raman spectra Q.) while the possibility of studying scattering from small sample volumes in the focussed laser beam (-100 pm diameter) can provide information on localized changes in chemical structure. 

Raman spectroscopy is considered a complementary technique to FTIR for the conformational analysis of chromatographic materials. Raman spectroscopy relies on... 

Ho, M. and Pemberton, J.E., Alkyl chain conformation of octadecylsilane stationary phases by Raman spectroscopy. 1. Temperature dependence. Anal. Chem., 70, 4915,... 

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... 

In addition, any rational approach to peptide hormone and neurotransmitter design must ultimately depend on the application of physical-chemical principles of conformation and structure, the use of various spectroscopic methods (especially nuclear magnetic resonance, circular dlchrolsm, and Raman spectroscopies. X-ray analysis where possible, etc.), and an understanding of the nature of a hormone-receptor Interaction In physical-chemical terms. Here again the use of conformatlonally restricted peptide structures Is critical (, 2. Recently we have... 

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