Secondary structure adopted by the Gly-Gly-X repetitive regions of dragline spider silk

Geoffrey M. Gray, Arjan van der Vaart, Chengchen Guo, Justin Jones, David Onofrei, Brian Cherry, Randolph V. Lewis, Jeffery Yarger, Gregory P. Holland

Research output: Contribution to journalArticle

12 Scopus citations

Abstract

Solid-state NMR and molecular dynamics (MD) simulations are presented to help elucidate the molecular secondary structure of poly(Gly-Gly-X), which is one of the most common structural repetitive motifs found in orb-weaving dragline spider silk proteins. The combination of NMR and computational experiments provides insight into the molecular secondary structure of poly(Gly-Gly-X) segments and provides further support that these regions are disordered and primarily non- β-sheet. Furthermore, the combination of NMR and MD simulations illustrate the possibility for several secondary structural elements in the poly(Gly-Gly-X) regions of dragline silks, including β-turns, 310-helicies, and coil structures with a negligible population of β-helix observed.

Original languageEnglish (US)
Article number2023
JournalInternational journal of molecular sciences
Volume17
Issue number12
DOIs
StatePublished - Dec 2 2016

    Fingerprint

Keywords

  • Molecular dynamics
  • NMR
  • Secondary structure
  • Solid-state NMR
  • Spider silk

ASJC Scopus subject areas

  • Catalysis
  • Molecular Biology
  • Spectroscopy
  • Computer Science Applications
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry

Cite this

Gray, G. M., van der Vaart, A., Guo, C., Jones, J., Onofrei, D., Cherry, B., Lewis, R. V., Yarger, J., & Holland, G. P. (2016). Secondary structure adopted by the Gly-Gly-X repetitive regions of dragline spider silk. International journal of molecular sciences, 17(12), [2023]. https://doi.org/10.3390/ijms17122023