Abstract
Infrared spectroscopy has been of limited usefulness in the study of complex biological systems for some or all of the following reasons: 1. Biological systems are generally dilute aqueous solutions. Thus, spectra of biological systems were run either in H<sub>2</sub>O (or D<sub>2</sub>O) with a resulting loss of large areas of the spectra because of the strong H<sub>2</sub>O (D<sub>2</sub>O) absorptions, or the spectra were run after removal of the water, which usually brings about major changes in the biological system. The use of thin cells to minimize the H<sub>2</sub>O or D<sub>2</sub>O absorption is not possible because "real-life" biological systems generally have a low solute concentration. The use of D<sub>2</sub>O posed additional problems because of hydrogen-deuterium exchange. 2. Biological systems generally contain many different species of proteins and, in such protein mixtures, variations in individual proteins or conformation changes can be difficult to identify by infrared spectroscopy especially when the changes only represent a small portion of the proteins. Thus, many infrared studies were of model systems containing a single protein species. 3. Biological systems contain numerous other organic species (besides proteins) which can have interfering infrared bands.
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