Secondary structure of chorion proteins of the teleostean fish Dentex dentex by ATR FT-IR and FT-Raman spectroscopy.
FT-Raman spectroscopy and ATR-IR spectroscopy were applied to study the secondary structure of the eggshell (chorion) proteins of the teleostean fish Dentex dentex. Raman and IR spectra clearly indicate an abundance of antiparallel beta-pleated sheet conformation in chorion proteins. This finding is further supported by analysis of the vibrational data by regression techniques and deconvolution procedures. Thus, the common morphological characteristics of D. dentex, Salmo gairdneri, and other teleostean fish chorions may be explained on the basis of common secondary structure features of their constituent proteins. A detailed understanding of the interactions that dictate the self-assembly of fish chorion proteins to form the fish eggshell awaits determination of amino acid sequences.
Iconomidou
V A
VA
Department of Cell Biology and Biophysics, Faculty of Biology, University of Athens, Athens 157 01, Greece.
Chryssikos
D G
DG
Gionis
V
V
Pavlidis
M A
MA
Paipetis
A
A
Hamodrakas
S J
SJ
D000818:Animals; D004527:Egg Proteins / Q000737:chemistry*; D005399:Fishes / Q000378:metabolism*; D008855:Microscopy, Electron, Scanning; D017433:Protein Structure, Secondary; D017550:Spectroscopy, Fourier Transform Infrared; D013059:Spectrum Analysis, Raman
D004527:Egg Proteins; C015753:chorion proteins