Secondary Structure Adopted by the Gly-Gly-X Repetitive Regions of Dragline Spider Silk

• Published in: International journal of molecular sciences 2016-12, Vol.17 (12), p.2023-2023
• Main Authors: Gray, Geoffrey M, van der Vaart, Arjan, Guo, Chengchen, Jones, Justin, Onofrei, David, Cherry, Brian R, Lewis, Randolph V, Yarger, Jeffery L, Holland, Gregory P
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Araneae; Fibroins - chemistry; Molecular biology; molecular dynamics; Molecular Dynamics Simulation; NMR; Nuclear magnetic resonance; Nuclear Magnetic Resonance, Biomolecular; Protein Structure, Secondary; Repetitive Sequences, Amino Acid; secondary structure; Silk; Simulation; solid-state NMR; spider silk
• ISSN: 1422-0067; 1661-6596; 1422-0067
• DOI: 10.3390/ijms17122023

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, 3 -helicies, and coil structures with a negligible population of α-helix observed.