Fourier-transform infrared spectroscopy conformation

Gordon, L.M., Lee, K.Y.C., Lipp, M.M., Zasadzinski, J.A., Walther, F.J., Sherman, M. A., and Waring, A.J. Conformational mapping of the N-terminal segment of surfactant protein B in lipid using C-13-enhanced Fourier transform infrared spectroscopy. J. Peptide Res. 

The conformational changes which have been described so far are probably all relatively small local changes in the structure of H,K-ATPase. This has been confirmed by Mitchell et al. [101] who demonstrated by Fourier transform infrared spectroscopy that a gross change in the protein secondary structure does not occur upon a conformational change from Ei to 3. Circular dichroism measurements, however [102,103], indicated an increase in a-helical structure upon addition of ATP to H,K-ATPase in the presence of Mg and... 

Prestrelski, S. J., Pikal, K., Arakawa, T. Optimization of lyophilization conditions for recombinant interleukin-2 by dried state conformational analysis using Fourier-transform infrared spectroscopy. Pharm. Res. 12 (9), p. 1250-1259, 1995... 

Chen, X., Knight, D. P., Shao, Z. Z., and Vollrath, F. (2002). Conformation transition in silk protein films monitored by time-resolved Fourier transform infrared spectroscopy Effect of potassium ions on Nephila spidroin films. Biochemistry 41, 14944-14950. 

One of the initial spectroscopic methods applied to stationary-phase characterization was Fourier transform infrared spectroscopy (FTIR). This originated from several important studies of phase conformational order in crystalline n-alkanes conducted in the late 1960s and early 1980s by Snyder, Maroncelli, and coworkers [111-114], In this work, assignments of C—H bond wagging modes were associated with chain... 

Srinivasan, G., Neumann-Singh, S., and Muller, K., Conformational order of n-alkyl modified silica gels as evaluated by Fourier transform infrared spectroscopy, J. Chromatogr. A, 1074, 31, 2005. 

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... 

The wavelengths of IR absorption bands are characteristic of specific types of chemical bonds. In the past infrared had little application in protein analysis due to instrumentation and interpretation limitations. The development of Fourier transform infrared spectroscopy (FUR) makes it possible to characterize proteins using IR techniques (Surewicz et al. 1993). Several IR absorption regions are important for protein analysis. The amide I groups in proteins have a vibration absorption frequency of 1630-1670 cm. Secondary structures of proteins such as alpha(a)-helix and beta(P)-sheet have amide absorptions of 1645-1660 cm-1 and 1665-1680 cm, respectively. Random coil has absorptions in the range of 1660-1670 cm These characterization criteria come from studies of model polypeptides with known secondary structures. Thus, FTIR is useful in conformational analysis of peptides and proteins (Arrondo et al. 1993). 

Breton, J., Bibikova, M., Oesterhelt, D., and Nabedryk, E., 1999, Conformational heterogeneity of the bacteriopheophytin electron acceptor in reaction centers from Rhodopseudomonas viridis revealed by Fourier transform infrared spectroscopy and site-directed mutagenesis. Biochemistry, 38 11541nll552. 

For molecular properties of the TAG polymorphs, local molecular structural information such as methyl-end group, olefinic conformation, and chain-chain interaction are unveiled by infrared (IR) spectroscopy, especially Fourier-transformed infrared spectroscopy (FT-IR) (23, 24). Compared with a pioneering work by Chapman (25), great progress has been achieved by using various FT-IR techniques, such as polarized transmission FT-IR, reflection absorption spectroscopy (RAS), and attenuated total reflection (ATR) (26-28). 

Fourier transform infrared spectroscopy also provides information about conformation of bofh hydrocarbon chains and head groups. EPR spectios-copy (Box 8-C) with doxyl probes on carbon atoms at different depths within the bilayer has also been em-ployed. ... 

Oximes and oxime ethers exist as a mixture of E and Z isomers with a relatively low difference of AG° and a moderate energy barrier to isomerization (<10 kcal mol-1) [28]. They show some similarities with imines and may interconvert at room temperature, spontaneously, by an acid- or base-catalyzed isomerization involving a nitronium ion, and photochemically [29,30]. Oxime ethers have been employed as amide surrogates in peptides where they display a marked Z-E isomerism which is mainly controlled by the formation of H-bonds, which stabilize a given isomer. As an example, the structure of pseudopeptide 6 was investigated by Fourier transform infrared spectroscopy (FTIR) and NMR spectroscopy which both showed that Z-6 is folded in a /Mike conformation by a strong bifurcate hydrogen bond whereas the E isomer adopts an extended conformation (Fig. 13.5) [31]. 

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