Abstract
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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 2039-2043 |
| Number of pages | 5 |
| Journal | Biomacromolecules |
| Volume | 11 |
| Issue number | 8 |
| DOIs | |
| State | Published - Aug 9 2010 |
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ASJC Scopus subject areas
- Bioengineering
- Materials Chemistry
- Polymers and Plastics
- Biomaterials
Cite this
Solid-state NMR comparison of various spiders' dragline silk fiber. / Creager, Melinda S.; Jenkins, Janelle E.; Thagard-Yeaman, Leigh A.; Brooks, Amanda E.; Jones, Justin A.; Lewis, Randolph V.; Holland, Gregory P.; Yarger, Jeffery.
In: Biomacromolecules, Vol. 11, No. 8, 09.08.2010, p. 2039-2043.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Solid-state NMR comparison of various spiders' dragline silk fiber
AU - Creager, Melinda S.
AU - Jenkins, Janelle E.
AU - Thagard-Yeaman, Leigh A.
AU - Brooks, Amanda E.
AU - Jones, Justin A.
AU - Lewis, Randolph V.
AU - Holland, Gregory P.
AU - Yarger, Jeffery
PY - 2010/8/9
Y1 - 2010/8/9
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=77955563006&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=77955563006&partnerID=8YFLogxK
U2 - 10.1021/bm100399x
DO - 10.1021/bm100399x
M3 - Article
C2 - 20593757
AN - SCOPUS:77955563006
VL - 11
SP - 2039
EP - 2043
JO - Biomacromolecules
JF - Biomacromolecules
SN - 1525-7797
IS - 8
ER -