Investigation of higher order structures of proteins by ultraviolet resonance Raman spectroscopy.
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.
Kitagawa
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Institute for Molecular Science, Okazaki National Research Institutes, Japan.
D000595:Amino Acid Sequence; D006454:Hemoglobins / Q000737:chemistry; D006801:Humans; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D015394:Molecular Structure; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D013056:Spectrophotometry, Ultraviolet; D013059:Spectrum Analysis, Raman
D006454:Hemoglobins; D046911:Macromolecular Substances; D011506:Proteins