Article
Secondary Structure Adopted by the Gly-Gly-X Repetitive Regions of Dragline Spider Silk
International Journal of Molecular Sciences
Document Type
Article
Publication Date
12-2-2016
Keywords
- Amino Acid Sequence,
- Animals,
- Fibroins,
- Molecular Dynamics Simulation,
- Nuclear Magnetic Resonance,
- Biomolecular,
- Protein Structure,
- Secondary,
- Repetitive Sequences,
- Amino Acid
Digital Object Identifier (DOI)
https://doi.org/10.3390/ijms17122023
Disciplines
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, 3
Rights Information
Creative Commons Attribution 4.0
Citation / Publisher Attribution
International Journal of Molecular Sciences, v. 17, issue 12, art. 2023
Citation Information
Geoffrey M Gray, Arjan van der Vaart, Chengchen Guo, Justin Jones, et al.. "Secondary Structure Adopted by the Gly-Gly-X Repetitive Regions of Dragline Spider Silk" International Journal of Molecular Sciences Vol. 17 Iss. 12 (2016) Available at: http://works.bepress.com/justin-jones/28/