Secondary Structure Adopted by the Gly-Gly-X Repetitive Regions of Dragline Spider Silk
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 α-helix observed.
- Author (aut): Gray, Geoffrey M.
- Author (aut): van der Vaart, Arjan
- Author (aut): Guo, Chengchen
- Author (aut): Jones, Justin
- Author (aut): Onofrei, David
- Author (aut): Cherry, Brian
- Author (aut): Lewis, Randolph V.
- Author (aut): Yarger, Jeffery
- Author (aut): Holland, Gregory P.
- Contributor (ctb): College of Liberal Arts and Sciences