Raman spectra of proteins

The C—S and S—S stretch vibrations of disulfides (Edsall et al., 1950) can be observed in the Raman spectra of proteins, but their interpretation is still somewhat controversial (see, for example, Klis and Siemion, 1978 Spiro and Gaber, 1977). Using series of model compounds, Van Wart et al. (1973) have related S—S stretch frequency to the xs (C/3—S—S—Cfi ) dihedral angle, while Sugeta et al. (1972, 1973) have related the S—S frequency to the x (Car—Cj8—S—S) di-... 

Both amide I and amide III bands are seen in Raman spectra of proteins.30 Lippert et al. devised the following method for estimating the fractions of a-helix, (3 sheet, and random coil conformations in proteins.31 The amide I Raman bands are recorded at 1632 and 1660 cm 1 in DzO (amide I ). The amide III band, which is weak in DzO, is measured at 1240 cm-1 in H20. The intensities of the three bands relative to the intensity of an internal standard (the 1448 cm 1 CH2... 

I. Harada and H. Takeuchi, Raman and ultraviolet resonance Raman spectra of proteins and related compounds, in Advances in Spectroscopy (R. A. H. Clark and R. E. Hester, eds.), Vol. 13, John Wiley, New York, 1986. 

Infrared spectra of proteins may be obtained either in the solid state (KBr pellets, crystals, or by diffuse reflectance techniques (Yang et al., 1985)) or in solution (D2O solutions, ATR techniques, as in the case of protein adsorption studies (Gendreau et al., 1982 Sec. 6.4). Raman spectra of proteins are usually obtained in solution. 

Kurouski, D., Postiglione, T, Deckert-Gaudig, X, Deckert, V., and Lednev, I.K. (2013) Amide I vibrational mode suppression in surface (SERS) and tip (TERS) enhanced Raman spectra of protein specimens. Analyst, 138, 1665-1673. doi 10.1039/C2AN36478F... 

Blum, C. et al (2012) Missing amide I mode in gap-mode tip-enhanced Raman spectra of proteins. /. Phys. Chem. C, 116, 23061-23066. doi 10.1021/)p306831p... 

The v4 region enhancement and structure in the resonance Raman spectra of xanthophylls reviewed in this chapter shows that it can be used for the analysis of carotenoid-protein interactions. Figure 7.8 summarizes the spectra for all four major types of LHCII xanthophylls. Lutein 2 possesses the most intense and well-resolved v4 bands. The spectrum for zeaxanthin is very similar to that of lutein with a slightly more complex structure. This similarity correlates with the structural similarity between these pigments. It is likely that they are both similarly distorted. The richer structure of zeaxanthin spectrum may be explained by the presence of the two flexible P-end rings... 

Spiro TG, Czernuszewicz RS, Han S. 1988. Iron-sulfur proteins and analog complexes, In Spiro TG, editor. Resonance Raman spectra of heme and metallopro-teins. New York WUey. p 523-54. 

Figure 5. Resonance Raman spectra of oxyhemerythrln with 0-16 (upper) and 0-18 (lower) In the oxo bridge. Protein (1.2 mM) and Na2S0 (0.3 M) maintained at 5 C In a flow cell and probed with 363.8 nm excitation. (Reproduced from Ref. 34. Copyright 1984 American Chemical Society.)...

Nakamoto, K. Infrared and Raman Spectra of Inorganic and Coordination Compounds Wlley-Intersclence New York, 1986. Long, D. A. Raman Spectroscopy McGraw-Hill New York, 1977. Loehr, T. M. Sanders-Loehr, J. In Copper Proteins and Copper Enzymes Lontle, R., Ed. CRC Press Boca Raton, 1984 pp. 115-155. 

The metaiioporphyrins form a diverse class of molecules exhibiting complex and varied photochemistries. Until recently time-resolved absorption and fluorescence spectroscopies were the only methods used to study metailoporphyrln excited state relaxation in a submicrosecond regime. In this paper we present the first picosecond time-resolved resonance Raman spectra of excited state metaiioporphyrins outside of a protein matrix. The inherent molecular specificity of resonance Raman scattering provides for a direct probe of bond strengths, geometries, and ligation states of photoexcited metaiioporphyrins. 

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... 

Resonance Raman spectra of one-iron preparations of uteroferrin and the splenic acid phosphatase show that tyrosine is a ligand.826 The intense visible spectra of these proteins is due to tyrosine - Fem charge-transfer transitions. Two or three tyrosine residues are implicated. 

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