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Proceedings Paper

UV resonance Raman spectroscopic study of Trp residues in a hydrophobic environment
Author(s): R. G. Efremov; Alexei V. Feofanov; Igor R. Nabiev
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Paper 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.

Paper Details

Date Published: 1 May 1991
PDF: 3 pages
Proc. SPIE 1403, Laser Applications in Life Sciences, (1 May 1991); doi: 10.1117/12.57381
Show Author Affiliations
R. G. Efremov, M. M. Shemyakin Institute of Bio-organic Chemistry (Russia)
Alexei V. Feofanov, M. M. Shemyakin Institute of Bio-organic Chemistry (Russia)
Igor R. Nabiev, M. M. Shemyakin Institute of Bio-organic Chemistry (Russia)


Published in SPIE Proceedings Vol. 1403:
Laser Applications in Life Sciences

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