Fourier Transform Infrared Spectrometry proteins

Table 5.7 Theoretically predicted polypeptides from the trypsin digestion of S-lacto-globulin (/3LG) . Reprinted from J. Chromatogr., A, 763, Turula, V. E., Bishop, R. T., Ricker, R. D. and de Haseth, J. A., Complete structure elucidation of a globular protein by particle beam liquid chromatography-Fourier transform infrared spectrometry and electrospray liquid chromatography-mass spectrometry - Sequence and conformation of /3-lactoglobulin , 91-103, Copyright (1997), with permission from Elsevier Science...

Kakuta, M., Hinsman, P., Manz, A., Lendl, B., Time-resolved Fourier transform infrared spectrometry using a microfabricated continuous flow mixer application to protein conformation study using the example of ubiquitin, Lab Chip 2003, 3, 82-85. 

The aim of this work is the determination of several nutritional parameters, such as Energetic Value, Protein, Fat, and Carbohydrates content, in commercially available yoghurt samples by using Attenuated Total Reflectance Fourier Transform Infrared (ATR-FT-IR) spectrometry and a partial least square approach. 

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]. 

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. 

Li, W. Hendrickson, C.L. Emmett, M.R. Marshall, A.G. Identification of Intact Proteins in Mixtures by Alternated Capillary Liquid Chromatography Electrospray Ionization and LC ESI Infrared Multiphoton Dissociation Fourier Transform Ion Cyclotron Resonance Mass Spectrometry, Anal. Chem. 71, 4397 402 (1999). 

Chapter 5 provides an overview of Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometry and its applications in the structural characterization of peptides and proteins. The principles of FT-ICR, that is, ion motion, ion excitation/ detection, and instrumental considerations, are discussed and an explanation of the features of FT-ICR that make it so suitable for peptide/protein analysis is presented. New methods for the fragmentation of peptide and protein ions in FT-ICR mass spectrometry, such as sustained off-resonance irradiation collision-induced dissociation (SORI-CID), infrared multiphoton dissociation (IRMPD), blackbody infrared radiative dissociation (BIRD), surface-induced dissociation (SID), and electron capture dissociation (BCD), are described in detail. Innovative hybrid FT-ICR instruments, which have recently become available, are reviewed. In conclusion, the chapter discusses the applications of FT-ICR in bottom-up and top-down proteomics. 

---