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Amide ir spectrum1/18/2024 Infrared spectroscopic evidence of conformational transitions of an atrial natriuretic peptide. Surewicz, W.K., Mantsch, H.H., Stahl, G.L. Fourier transform infrared studies of ribonuclease in H2O and 2H2O solutions. Olinger, J.M., Hill, D.M., Jakobsen, R.J. Protein conformation by infrared spectroscopy: resolution enhancement by Fourier self-deconvolution. Yang, W.-J., Griffiths, P.R., Byler, D.M. Second-derivative infrared spectroscopic studies of the secondary structures of bacteriorhodopsin and Ca2+-ATPase. Protein structure by Fourier transform infrared spectroscopy: second derivative spectra. Qualification of FTIR spectroscopic method for protein secondary structural analysis. Fourier transform infrared spectroscopic analysis of protein secondary structures. in Infrared Analysis of Peptides and Proteins Vol. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Determination of protein secondary structure using factor analysis of infrared spectra. Protein secondary structures in water from second-derivative amide I infrared spectra. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Resolution-enhanced Fourier transform infrared spectroscopy of enzymes. Solvent denaturation of proteins as observed by resolution-enhanced Fourier transform infrared spectroscopy. Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy. Using Fourier transform IR spectroscopy to analyze biological materials. Small amounts of high-purity (>95%) proteins at high concentrations (>3 mg ml −1) are needed in this protocol typically, the procedure can be completed in 1–2 d.īaker, M.J. In this protocol, we have detailed the principles that underlie the determination of protein secondary structure by FTIR spectroscopy, as well as the basic steps involved in protein sample preparation, instrument operation, FTIR spectra collection and spectra analysis in order to estimate protein secondary-structural components in aqueous (both H 2O and deuterium oxide (D 2O)) solution using algorithms, such as second-derivative, deconvolution and curve fitting. Amide I bands (1,700–1,600 cm −1) are the most prominent and sensitive vibrational bands of the protein backbone, and they relate to protein secondary structural components. The repeat units in proteins give rise to nine characteristic IR absorption bands (amides A, B and I–VII). The IR spectral data of polymers are usually interpreted in terms of the vibrations of a structural repeat. Fourier transform IR (FTIR) spectroscopy is a nondestructive technique for structural characterization of proteins and polypeptides.
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