Proteins Fourier-transform infrared spectroscopy

Prestrelski SJ, Byler DM, Liebman MN. Generation of a substructure library for the description and classification of protein secondary structure. II. Application to spectrastructure correlations in Fourier transform infrared spectroscopy. Proteins 1992 14 440-450. 

The sequence of a globular protein was confirmed by a combination of enzymatic digestion and HPLC with both Fourier-transform infrared spectroscopy (LC-FTIR spectroscopy) and mass spectrometry [11]. 

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... 

McGovern, A. C. Ernill, R. Kara, B. V. Kell, D. B. Goodacre, R. Rapid analysis of the expression of heterologous proteins in Escherichia coli using pyrolysis mass spectrometry and Fourier transform infrared spectroscopy with chemometrics Application to a2- interferon production. J. Biotechnol. 1999, 72,157-167. 

Varenne, A., Salmain, M., Brisson, C., and Jaouen, G. (1992) Transition metal carbonyl labeling of proteins. A novel approach to a solid-phase two-site immunoassay using Fourier transform infrared spectroscopy. Bioconjugate Chem. 3, 471-476. 

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. 

Vandenbussche G, Clercx A, Clercx M, et al. Secondary structure and orientation of the surfactant protein SP-B in a lipid environment. A Fourier transform infrared spectroscopy study. Biochemistry 1992 31(38) 9169-9176. 

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... 

Fourier transform infrared spectroscopy (FTIR) s Measures protein and carbohydrate vibrational, stretching, and bending energies... 

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). 

Arrondo, J.L., Muga, A., Castresana, J., Goni, F.M. (1993). Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy. Prog. Biophys. Molec. Biol., 59, 23-56. 

Surewicz, W.K., Mantsch, H.H., Chapman, D. (1993). Determination of protein secondary structure by Fourier transform infrared spectroscopy A critical assessment. Biochemistry, 32, 389-394. 

Even though these approaches are powerful methods for determining functional sites on proteins, they are limited if not coupled with some form of structural determination. As Figure 2 illustrates, molecular biology and synthetic peptide/antibody approaches are not only interdependent, they are tied in with structural determination. Structural determination methods can take many forms, from the classic x-ray crystallography and NMR for three-dimensional determination, to two-dimensional methods such as circular dichroism and Fourier Transformed Infrared Spectroscopy, to predictive methods and modeling. A structural analysis is crucial to the interpretation of experimental results obtained from mutational and synthetic peptide/antibody techniques. 

Infant formula, tocopherol/tocotrienol analysis, 479, 487, 489 (table) Infrared spectroscopy, see also Fourier transform infrared spectroscopy fat measurement, 572 trans fatty acids, 505 Infrared/ultrasonic scanner for emulsion creaming, 597-598 Injection techniques for GC, 449 Insoluble recombinant proteins, purification of, 276... 

In THE PAST DECADE, IMPROVEMENTS IN infrared spectroscopic instrumentation have contributed to significant advances in the traditional analytical applications of the technique. Progress in the application of Fourier transform infrared spectroscopy to physiochemical studies of colloidal assemblies and interfaces has been more uneven, however. While much Fourier transform infrared spectroscopic work has been generated about the structure of lipid bilayers and vesicles, considerably less is available on the subjects of micelles, liquid crystals, or other structures adopted by synthetic surfactants in water. In the area of interfacial chemistry, much of the infrared spectroscopic work, both on the adsorption of polymers or proteins and on the adsorption of surfactants forming so called "self-assembled" mono- and multilayers, has transpired only in the last five years or so. 

The major peculiarities for a diagenetically altered bone are an increase in crystal size and a decrease in protein content [104], thus complementary information on the state of degradation can be obtained by FT-IR (Fourier transform infrared spectroscopy). The characteristic splitting of the double peak at 563-604 cm-1 corresponds to the phosphate vibrations v4 (P04)3- indicating mineral-phase modifications, e.g. changes in crystallinity. A low value for the splitting factor SF indicates a high amount of amorphous material in the mineral phase and was obtained as described in Ref. [105],... 

Fourier Transform Infrared Spectroscopy (FTIR) Studies. Infrared spectra of hairless mouse stratum corneum, lipid extract and protein residue are illustrated in Figures 3 and 4 for the 4000 to 2600 cm-2 and 1800 to 1360 cm-2 regions, respectively. 

S. J. Prestrelski, T. Arakawa, and J. F. Carpenter, The structure of proteins in lyophilized formulations using Fourier transform infrared spectroscopy, in Formulation and Delivery of Proteins and Peptides, (J. L. Cleland and R. Danger, eds.) American Chemical Society Symposium Series No. 567, 1994, pp. 148-169. 

Figure 12 The correlation of storage stability with protein structure as determined by Fourier transform infrared spectroscopy (FTIR) apparent first-order rate constants for aggregation of freeze dried rlL-2. (O) 45°C storage. ( ) 29°C storage. (Data from [67].)...

The secondary structure of proteins may also be assessed using vibrational spectroscopy, fourier transform infrared spectroscopy (FTIR), and Raman spectroscopy both provide information on the secondary structure of proteins. The bulk of the literature using vibrational spectroscopy to study protein structure has involved the use of FTIR. Water produces vibrational bands that interfere with the bands associated with proteins. For this reason, most of the FTIR literature focuses on the use of this technique to assess structure in the solid state or in the presence of non-aqueous environments. Recently, differential FTIR has been used in which a water background is subtracted from the FTIR spectrum. This workaround is limited to solutions containing relatively high protein concentrations. 

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