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1 May 1991 UV resonance Raman spectroscopic study of Trp residues in a hydrophobic environment
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Proceedings Volume 1403, Laser Applications in Life Sciences; (1991) https://doi.org/10.1117/12.57381
Event: Laser Applications in Life Sciences, 1990, Moscow, Russian Federation
Abstract
Resonance Raman (RR) spectroscopy with UV excitation is sensitive to the state of Tyr and Trp in proteins and permits analysis of the effects of their microenvironment upon the conformational transitions in biological processes. But interpretation of the spectral features is complicated due to the lack of information about the influence of the medium effects on RR data. The main factors which can change the intensities, bandwidths, and the positions of electronic-vibrational transitions of aromatic residues in protein and, therefore, can specifically perturb UV RR spectra, are: hydrophobicity of the environment, electrostatic interactions, and hydrogen bonding.
© (1991) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
R. G. Efremov, Alexei V. Feofanov, and Igor R. Nabiev "UV resonance Raman spectroscopic study of Trp residues in a hydrophobic environment", Proc. SPIE 1403, Laser Applications in Life Sciences, (1 May 1991); https://doi.org/10.1117/12.57381
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