LASER-RAMAN AND FT-IR SPECTROSCOPIC STUDIES OF PEPTIDE-ANALOGS OF SILKMOTH CHORION PROTEIN SEGMENTS

Citation
Dc. Benaki et al., LASER-RAMAN AND FT-IR SPECTROSCOPIC STUDIES OF PEPTIDE-ANALOGS OF SILKMOTH CHORION PROTEIN SEGMENTS, International journal of biological macromolecules, 23(1), 1998, pp. 49-59
Citations number
24
Categorie Soggetti
Biology
ISSN journal
01418130
Volume
23
Issue
1
Year of publication
1998
Pages
49 - 59
Database
ISI
SICI code
0141-8130(1998)23:1<49:LAFSSO>2.0.ZU;2-#
Abstract
Silkmoth chorion, the proteinaceous major component of the eggshell, w ith extraordinary mechanical and physiological properties, consists of a complex set of proteins, which have a tripartite structure: a centr al, evolutionarily conserved, domain and two more variable 'arms'. Pep tide-analogues of silkmoth chorion protein central domain segments hav e been synthesized. Laser-Raman and infrared spectroscopic studies sug gest the preponderance of antiparallel beta-pleated sheet structure fo r these peptides, both in solution and in the solid state. (C) 1998 El sevier Science B.V. All rights reserved.