[An analysis of the secondary structure of spider spidroins I and II belonging to different species].
We have analyzed the secondary structure of spidroin proteins of I and II types, related to spiders of different species. We used standard methods of secondary structure prediction NNPREDICT and JPRED and also analyzed the occurrences of oligopeptides with a preferred secondary structure with the help of the OLIGON program. We have demonstrated that local segments of the polypeptide chain can adopt alpha- and beta-conformations as well as the left-handed helix of polyproline II type. Periodical patterns found in the amino acid distribution indicate that there is a possibility of development of a macroscopic order accompanied by local conformational transitions.
Ragulina
L E
LE
Makeev
V Iu
VIu
Esipova
N G
NG
Tumanian
V G
VG
Vlasov
P K
PK
Bogush
V G
VG
Debabov
V G
VG
D000595:Amino Acid Sequence; D000818:Animals; D005349:Fibroins / Q000737:chemistry*; D019476:Insect Proteins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D047011:Silk / Q000737:chemistry*; D013045:Species Specificity; D013112:Spiders / Q000737:chemistry
D019476:Insect Proteins; D047011:Silk; C086087:spidroin 1; C076815:spidroin 2; D005349:Fibroins