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- W2000259357 abstract "UV Raman spectroscopy is a powerful tool for investigating the structures and interactions of the aromatic side chains of Phe, Tyr, Trp, and His in proteins. This is because Raman bands of aromatic ring vibrations are selectively enhanced with UV excitation, and intensities and wavenumbers of Raman bands sensitively reflect structures and interactions. Interpretation of protein Raman spectra is greatly assisted by using empirical correlations between spectra and structure. Many Raman bands of aromatic side chains have been proposed to be useful as markers of structures and interactions on the basis of empirical correlations. This article reviews the usefulness and limitations of the Raman markers for protonation/deprotonation, conformation, metal coordination, environmental polarity, hydrogen bonding, hydrophobic interaction, and cation-π interaction of the aromatic side chains. The utility of Raman markers is demonstrated through an application to the structural analysis of a membrane-bound proton channel protein." @default.
- W2000259357 created "2016-06-24" @default.
- W2000259357 creator A5052552300 @default.
- W2000259357 date "2011-11-01" @default.
- W2000259357 modified "2023-09-27" @default.
- W2000259357 title "UV Raman Markers for Structural Analysis of Aromatic Side Chains in Proteins" @default.
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- W2000259357 doi "https://doi.org/10.2116/analsci.27.1077" @default.
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