Abstract
Progress in laser technology and light detection devices have enabled us to explore protein structures and their dynamics by using time-resolved resonance Raman spectroscopy. It is in the last decade that Raman spectra of proteins excited at 200–240 nm have brought about rich structural information. The technological developments in deep UV resonance Raman spectroscopy are reviewed first, and the unique information on proteins obtainable from such spectra are summarized. As an application of this technique to investigations of the higher order structures of proteins, studies on the quaternary structure transition of haemoglobin are described.
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