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Proceedings Paper

Study of protein structure in insect virus (PrGV) by laser Raman spectroscopy
Author(s): PeiDi Bao; XinMing Liu; TianQuan Huang; Shi Gui Liu
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Paper Abstract

We report here our observation of Raman spectrum of the Granulosis Virus of cabbage butterfly Preris rapae (PrGV) and investigate the protein structure of the inclusion body of PrGV. The intense Amide III line at 1248 cm-1 and Amide I line at 1668 cm-1 in the Raman spectrum of PrGV contains a predominantly random-Coil or (beta) -turn secondary structure. The intensities ratio of the tyrosyl lines 850 cm-1 and 830 cm-1 was found to be 1.25, it indicates the tyrosyl residues are exposed to a solvent. According to s-s stretching vibration frequency 509 cm-1, the protein molecules of PrGV have gauche-gauche-gauche linkage. The strong peak at 1367 cm-1 is typical of Tryptophans buried in a hydrophobic environment.

Paper Details

Date Published: 1 May 1993
PDF: 3 pages
Proc. SPIE 1890, Biomolecular Spectroscopy III, (1 May 1993); doi: 10.1117/12.145253
Show Author Affiliations
PeiDi Bao, Sichuan Univ. (China)
XinMing Liu, Sichuan Univ. (China)
TianQuan Huang, Sichuan Univ. (China)
Shi Gui Liu, Sichuan Univ. (China)

Published in SPIE Proceedings Vol. 1890:
Biomolecular Spectroscopy III
Laurence A. Nafie; Henry H. Mantsch, Editor(s)

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