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Proceedings Paper

Near-infrared FT-Raman study of denatured proteins produced under high pressure and temperature
Author(s): Yukihiro Ozaki; R. K. Cho; J. J. Ahn
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Paper Abstract

Near-infrared (NIR) excited FT-Raman spectra were measured for intact, modified, and denatured lysozyme in solid states. The following conclusions could be reached from the Raman measurements. (1) FT-Raman spectrum of lysozyme treated at 90 degree(s)C and 10000 kPa is very close to that of the intact protein; only a slight shift of amide I band is observed. (2) Heat denaturation is clearly detected in the Raman spectrum for the protein treated at 120 degree(s)C; the Raman spectral changes suggest that most (alpha) -helix structure change into random coil structure upon the heat denaturation at 120 degree(s)C. (3) FT-Raman spectrum of lysozyme modified by glucose is close to that of intact lysozyme, indicating that the modification does not cause a marked secondary structure change. (4) The FT-Raman spectrum of the modified lysozyme by glucose treated at 120 degree(s)C and 15000 kPa is somewhat different in the amide I and III regions from that of the denatured lysozyme, suggesting that secondary structural changes caused by the heat denaturation are different from each other between the two denatured proteins.

Paper Details

Date Published: 17 June 1993
PDF: 5 pages
Proc. SPIE 1921, Laser Spectroscopy of Biomolecules, (17 June 1993); doi: 10.1117/12.146136
Show Author Affiliations
Yukihiro Ozaki, Kwansei Gakuin Univ. (Japan)
R. K. Cho, Kyung-pook National Univ. (South Korea)
J. J. Ahn, Kyung-pook National Univ. (South Korea)

Published in SPIE Proceedings Vol. 1921:
Laser Spectroscopy of Biomolecules

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