Orientation, structure, wet-spinning, and molecular basis for supercontraction of spider dragline silk.
This manuscript reviews work from our laboratory that addresses the orientation, secondary structure, wet-spinning, and molecular basis for supercontraction of spider silk. It identifies the poly(alanine) runs as the crystalline regions, establishes the degree of orientation of these regions, and identifies the secondary structural elements of the conserved L-G-X-Q (X = G, S, or N) regions. It also describes methods for spinning very small amounts of protein polymers and it sets forth several molecular-level hypotheses concerning supercontraction.
Jelinski
L W
LW
Center for Advanced Technology in Biotechnology, Cornell University, Ithaca, NY 14853, USA.
Blye
A
A
Liivak
O
O
Michal
C
C
LaVerde
G
G
Seidel
A
A
Shah
N
N
Yang
Z
Z
D000595:Amino Acid Sequence; D000818:Animals; D003285:Contractile Proteins / Q000737:chemistry*; D019476:Insect Proteins / Q000737:chemistry* / Q000648:ultrastructure; D008855:Microscopy, Electron, Scanning; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D047011:Silk; D012997:Solvents; D013112:Spiders / Q000737:chemistry*; D013312:Stress, Physiological; D014867:Water / Q000737:chemistry
D003285:Contractile Proteins; D019476:Insect Proteins; D047011:Silk; D012997:Solvents; D014867:Water