Molecular orientation and two-component nature of the crystalline fraction of spider dragline silk.
The molecular origin of the exceptional mechanical properties of spider silk is unclear. This paper presents solid-state 2H nuclear magnetic resonance data from unoriented, oriented, and supercontracted fibers, indicating that the crystalline fraction of dragline silk consists of two types of alanine-rich regions, one that is highly oriented and one that is poorly oriented and less densely packed. A new model for the molecular-level structure of individual silk molecules and their arrangement in the fibers is proposed. These data suggest that it will be necessary to control the secondary structure of individual polymer molecules in order to obtain optimum properties in bio-inspired polymers.
Center for Advanced Technology in Biotechnology, Cornell University, Ithaca, NY 14853, USA.
A H
AH
Simmons
C A
CA
Michal
L W
LW
Jelinski
D000409:Alanine / Q000032:analysis; D000465:Algorithms; D000595:Amino Acid Sequence; D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D005349:Fibroins; D005998:Glycine / Q000032:analysis; D019476:Insect Proteins; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000032:analysis; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D047011:Silk; D013112:Spiders / Q000737:chemistry*
D019476:Insect Proteins; D010455:Peptides; D011506:Proteins; D047011:Silk; C076815:spidroin 2; C019529:polyalanine; D005349:Fibroins; D000409:Alanine; D005998:Glycine