[Left helix of polyproline II type and genesis of beta-structures in spidroins 1 and 2 and their recombinant analogs].
The distribution of secondary structures along the polypeptide chains of spider proteins spidroins 1 and 2 and their recombinant analogs has been studied by statistical methods. It was found that these proteins in the monomolecular form contain only trace amounts of beta-structures. At the same time, the regions of the sequence including Ala and Gly are predicted as helical-containing (with alpha-helices and left-helices of polyproline II type). An analysis of literature data and our data obtained in this study shows that the main conformation of the polypeptide chain solutions of spidroins 1 and 2 and their recombinant analogs in water solutions is the left-helix of polyproline II type with some contaminations of alpha-helices and a very small share of beta-structures. The transition to the state with extended conformations, which are peculiar to mature filaments of spider webs, requires the dehydration of the polypeptide chain backbone. Thus, the genesis of beta-structure in spider web proteins is determined by the conditions of conformation transitions between the main regular conformations of the polypeptide chain backbone.
Esipova
N G
NG
Ragulina
L E
LE
Davydova
L I
LI
Lobachev
V M
VM
Makeev
V Iu
VIu
Bogush
V G
VG
Tumanian
V G
VG
Debabov
V G
VG
D000595:Amino Acid Sequence; D000818:Animals; D005349:Fibroins / Q000737:chemistry*; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry; D013112:Spiders
D010455:Peptides; D011994:Recombinant Proteins; C086087:spidroin 1; C076815:spidroin 2; C011083:polyproline; D005349:Fibroins