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Laser-Raman spectroscopic studies of the eggshell (chorion) of Bombyx mori
Authors:SJ Hamodrakas  EI Kamitsos  A Papanikolaou
Institution:

a Department of Biochemistry, Cellular and Molecular Biology and Genetics, University of Athens, Panepistimiopolis, Kouponia, Athens 157.01, Greece

b Institute of Theoretical and Physical Chemistry, The National Hellenic Research Foundation, 48 Vassileos Constantinou Ave., Athens 501.1, Greece

Abstract:Laser-Raman spectroscopic studies of the eggshell (chorion) of the silkmoth Bombyx mori reveal that its component proteins consist of 60–70% antiparallel β-pleated sheet and 30–40% of β-turns. The disulphide bonds, which crosslink the (extremely rich in cysteine)-proteins of the outer lamellar eggshell layer, are apparently found in G-G-G (gauche-gauche-gauche) and T-G-T (trans-gauche-trans) conformation; there is no evidence for the existence of free sulphydryls. The highly localized tyrosine residues appear to form hydrogen bonds, acting as weak proton donors or as acceptors.
Keywords:Eggshell  chorion  structural protein  laser-Raman spectroscopy  secondary structure determination  disulphide bonds
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