Protein Dynamics From UV Resonance Raman Spectroscopy

Abstract

The advent of reliable pulsed lasers whose frequency can be shifted into the ultraviolet region has made possible the application of ultraviolet resonance Raman (UVRR) spectroscopy to proteins. Appropriate tuning of the laser yields selective enhancement of vibrational modes of the aromatic side chains phenylalanine, tyrosine and tryptophan, or of the amide bonds [1–3]. The amide UVRR bands are responsive to the protein secondary structure. Enhancements of the classic amide II and III bands decrease with increasing α-helical content, [4] as does an additional UVRR band, amide S [5–8]. The aromatic side chain UVRR bands show frequency and/or intensity changes in response to changes in their local environment, particularly to H-bonding changes [9–12]. They can therefore monitor protein conformation changes that alter the tertiary or quaternary structure.KeywordsProtein Secondary StructureAromatic Side ChainExcitation ProfileOptimum Excitation WavelengthHeme Binding PocketThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.