Quantitative correlation between the protein primary sequences and secondary structures in spider dragline silks

Janelle E. Jenkins, Melinda S. Creager, Randolph V. Lewis, Gregory P. Holland, Jeffery L. Yarger

Research output: Contribution to journalArticle

84 Citations (Scopus)

Abstract

Synthetic spider silk holds great potential for use in various applications spanning medical uses to ultra lightweight armor; however, producing synthetic fibers with mechanical properties comparable to natural spider silk has eluded the scientific community. Natural dragline spider silks are commonly made from proteins that contain highly repetitive amino acid motifs, adopting an array of secondary structures. Before further advances can be made in the production of synthetic fibers based on spider silk proteins, it is imperative to know the percentage of each amino acid in the protein that forms a specific secondary structure. Linking these percentages to the primary amino acid sequence of the protein will establish a structural foundation for synthetic silk. In this study, nuclear magnetic resonance (NMR) techniques are used to quantify the percentage of Ala, Gly, and Ser that form both β-sheet and helical secondary structures. The fraction of these three amino acids and their secondary structure are quantitatively correlated to the primary amino acid sequence for the proteins that comprise major and minor ampullate silk from the Nephila clavipes spider providing a blueprint for synthetic spider silks.

Original languageEnglish (US)
Pages (from-to)192-200
Number of pages9
JournalBiomacromolecules
Volume11
Issue number1
DOIs
StatePublished - Jan 11 2010

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Silk
Proteins
Amino acids
Amino Acids
Synthetic fibers
Imino Acids
Blueprints
Armor
Medical applications
Nuclear magnetic resonance
Mechanical properties

ASJC Scopus subject areas

  • Bioengineering
  • Materials Chemistry
  • Polymers and Plastics
  • Biomaterials

Cite this

Quantitative correlation between the protein primary sequences and secondary structures in spider dragline silks. / Jenkins, Janelle E.; Creager, Melinda S.; Lewis, Randolph V.; Holland, Gregory P.; Yarger, Jeffery L.

In: Biomacromolecules, Vol. 11, No. 1, 11.01.2010, p. 192-200.

Research output: Contribution to journalArticle

Jenkins, Janelle E. ; Creager, Melinda S. ; Lewis, Randolph V. ; Holland, Gregory P. ; Yarger, Jeffery L. / Quantitative correlation between the protein primary sequences and secondary structures in spider dragline silks. In: Biomacromolecules. 2010 ; Vol. 11, No. 1. pp. 192-200.
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