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• W2473202220 startingPage "183" @default.
• W2473202220 abstract "Infrared spectroscopy was one of the earliest techniques to be used for the structural studies of polypeptides and proteins (1,2). However, a major difficulty that limited earlier studies of such biological molecules was the absorption of liquid H2O, which shows strong absorption over much of the fundamental region of the infrared spectrum. This severely limited the analysis of biological molecules in their native state, and necessitated the use of dry films, KBr disks, or D22O as a solvent. There is no strong absorption from D2O, in the region 1700–1500 cm-1and this spectral region is one which is particularly important for the study of polypeptides and proteins. The infrared spectra of liquid H2O and for comparison liquid D2O are shown in Fig. 1. The recent development of computerized FT-IR (Fourier transform infrared) instrumentation now permits the subtraction of background water absorptions from dilute samples (3,4) and, hence, enables the study of biomolecules in their more natural environment, e.g., H2O, buffer solutions, and so on. This approach has revolutionized the application of infrared spectroscopy for the study of biological molecules." @default.
• W2473202220 created "2016-07-22" @default.
• W2473202220 creator A5008012348 @default.
• W2473202220 creator A5020176415 @default.
• W2473202220 date "2003-11-14" @default.
• W2473202220 modified "2023-10-10" @default.
• W2473202220 title "Analysis of Polypeptide and Protein Structures Using Fourier Transform Infared Spectroscopy" @default.
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• W2473202220 doi "https://doi.org/10.1385/0-89603-232-9:183" @default.
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