Laser-Raman and FT-IR spectroscopic studies of peptide-analogues of silkmoth chorion protein segments.
Silkmoth chorion, the proteinaceous major component of the eggshell, with extraordinary mechanical and physiological properties, consists of a complex set of proteins, which have a tripartite structure: a central, evolutionarily conserved, domain and two more variable 'arms'. Peptide-analogues of silkmoth chorion protein central domain segments have been synthesized. Laser-Raman and infrared spectroscopic studies suggest the preponderance of antiparallel beta-pleated sheet structure for these peptides, both in solution and in the solid state.
Benaki
D C
DC
Department of Biology, University of Athens, Greece.
Aggeli
A
A
Chryssikos
G D
GD
Yiannopoulos
Y D
YD
Kamitsos
E I
EI
Brumley
E
E
Case
S T
ST
Boden
N
N
Hamodrakas
S J
SJ
D000595:Amino Acid Sequence; D000818:Animals; D012831:Bombyx / Q000737:chemistry* / Q000235:genetics; D002823:Chorion / Q000737:chemistry; D019476:Insect Proteins / Q000138:chemical synthesis / Q000737:chemistry* / Q000235:genetics; D007834:Lasers; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry / Q000235:genetics; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017550:Spectroscopy, Fourier Transform Infrared; D013059:Spectrum Analysis, Raman / Q000379:methods
D019476:Insect Proteins; D046911:Macromolecular Substances; D010446:Peptide Fragments