Abstract
This paper aims to review recent trends and developments in high-pressure FTIR studies on proteins. Methodological principles of research in this field, the assignment of the diagnostically-useful IR bands, as well as several examples illustrating the application of IR spectroscopy in high pressure studies on proteins are all within the scope of this article. This work is also an attempt to show that IR spectroscopy can find application not only for studies of the pressure-induced unfolding of protein structure, but also for the examination of minor unfolding events or local conformational changes induced by high pressure. A more elaborate discussion of the high-pressure study on bovine α-lactalbumin is also presented.
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