Solid-state NMR comparison of various spiders' dragline silk fiber.
Major ampullate (dragline) spider silk is a coveted biopolymer due to its combination of strength and extensibility. The dragline silk of different spiders have distinct mechanical properties that can be qualitatively correlated to the protein sequence. This study uses amino acid analysis and carbon-13 solid-state NMR to compare the molecular composition, structure, and dynamics of major ampullate dragline silk of four orb-web spider species ( Nephila clavipes , Araneus gemmoides , Argiope aurantia , and Argiope argentata ) and one cobweb species ( Latrodectus hesperus ). The mobility of the protein backbone and amino acid side chains in water exposed silk fibers is shown to correlate to the proline content. This implies that regions of major ampullate spidroin 2 protein, which is the only dragline silk protein with any significant proline content, become significantly hydrated in dragline spider silk.
Creager
Melinda S
MS
Department of Molecular Biology and Macromolecular Core Facility, University of Wyoming, Laramie, Wyoming 82071, USA.
Jenkins
Janelle E
JE
Thagard-Yeaman
Leigh A
LA
Brooks
Amanda E
AE
Jones
Justin A
JA
Lewis
Randolph V
RV
Holland
Gregory P
GP
Yarger
Jeffery L
JL
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002853:Chromatography, Liquid; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D047011:Silk / Q000737:chemistry*; D013045:Species Specificity; D013112:Spiders
D000596:Amino Acids; D047011:Silk